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(2E,6E,10Z)-3,7,11-trimethyl-12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodeca-2,6,10-trien-1-yl diphosphate + Rab7 GTPase
(2E,6E,10Z)-3,7,11-trimethyl-12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodeca-2,6,10-trien-1-yl-Rab7 GTPase + diphosphate
-
in vitro prenylation assay with 4 microM Rab7 wild type or mutants, 6 mircoM Rab escort protein, 6 microM enzyme, 50 mM HEPES buffer, pH 7.2, containing 50 mM NaCl, 5 mM dithioerythritol, 2 mM MgCl2, and 10 mircoM GDP, 25°C, 50 microM of the geranylgeranyl diphosphate analogue (3,7,11-trimethyl-12-(7-nitro-benzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,10-triem-1) diphosphate, end-point assay with 6 microM Rab7 wild type or mutants, 10 microM Rab escort protein, 6 microM enzyme in the same buffer mixture, and 40 microM (3,7,11-trimethyl-12-(7-nitro-benzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,10-triem-1) diphosphate, 1.5 hours at 25°C
-
-
?
(3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1) diphosphate + Rab7
(3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1)-Rab7 + diphosphate
-
geranylgeranyl diphosphate analogue and Rab7 as substrates in the presence of Rab escort protein, in vitro inhibition assays
-
-
?
biotinylated geranyl diphosphate + EYFP-Rab7
S-biotin-geranyl-Rab7 + diphosphate
-
COS-7 cells are transfected with EYFP-Rab7 fusion protein and incubated with inhibitors, cells lysed after 24 h, clarified supernatant incubated in biotinylated geranyl diphosphate (geranylgeranyl diphosphate substrate analogue), recombinant RabGGTase and Rab escort protein, in vivo inhibitor studies
-
-
?
geranylgeranyl diphosphate + Arabidopsis thaliana RAB-ATa protein
S-geranylgeranyl-RAB GTPase + diphosphate
-
homozygous insertion mutants (rgtb1-1 and rgtb1-2) of the major beta-subunit of Arabidopsis enzyme (RGTB1) lead to reduced enzyme activity (about 25%), 50 mM phosphate buffer, pH 7.6, 10 mM MgCl2, 5 mM DTT, 0.5 microM tritium-labelled all trans-geranylgeranyl pyrophosphate, 4 microg recombinant Arabidopsis thaliana RAB-A2a protein, 32°C, 40 min
-
-
?
geranylgeranyl diphosphate + FBXL2
geranylgeranyl-FBXL2 + diphosphate
FBXL2 is an ubiquitin-ligase
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
geranylgeranyl diphosphate + Rab
S-geranylgeranyl-Rab + diphosphate
-
His6- and gluthathione S-transferase-tagged Rab proteins such as canine Rab1a, human Rab27a, Rab5a, Rab18, Rab6a, Rab13, and mouse Rab23
-
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
geranylgeranyl diphosphate + Rab-protein-cysteine
S-geranylgeranyl-Rab-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + Rab1A
?
-
substrate motif: -XXCC
-
-
?
geranylgeranyl diphosphate + Rab1B
?
-
-
-
-
?
geranylgeranyl diphosphate + Rab3A
?
-
substrate motif: -XCXC
-
-
?
geranylgeranyl diphosphate + Rab5A
?
-
substrate motif: -CCXX
-
-
?
geranylgeranyl diphosphate + Rab7 protein
S-geranylgeranyl-Rab7 protein + diphosphate
-
the N-terminal Cys207 is preferred to Cys205, activity with Rab7 mutants, overview
-
-
?
geranylgeranyl diphosphate + Rab8
?
-
the Rab protein Rab8-GTPase, which end with a Cys-Val-Leu-Leu motif able to serve as a substrate for either geranylgeranyl transferase I and II, but modified predominantly by either geranylgeranyl transferase II in vitro, but the mutation of Y78D prevents Rab8 from serving as a substrate
-
-
?
geranylgeranyl diphosphate + Ypt1p
?
[3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)dodeca-2,6,10-trien-1] diphosphate + Rab7 protein
?
-
i.e. NBD-FPP, a fluorescent analogue of geranylgeranyl diphosphate, which is a lipid donor for RabGGTase
product is mono-NBD-farnesylated Rab7:REP-1 complex
-
?
additional information
?
-
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme attaches geranylgeranyl groups to two C-terminal cysteines in Ras-related GTPases of a single family, the Rab family, Ypt/Sec4 in lower eukaryotes, that terminate in XXCC, XCXC and CCXX motifs, reaction only if Rab is bound to a carrier protein termed Rab escort protein, REP
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
Rab protein forms a stable complex with Rab escort protein, REP
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
the Rab protein Rab8-GTPase, which end with a Cys-Val-Leu-Leu motif able to serve as a substrate for either geranylgeranyl transferase I and II, but modified predominantly by either geranylgeranyl transferase II in vivo
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
GDP-bound form of Rab3 is preferred substrate of enzyme
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
the enzyme catalyzes posttranslational modification of proteins, the farnesyl moieties attached to the substrates are directly involved in protein-protein interactions as well as in protein-membrane interactions
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
substrate motif: carboxy-terminal motifs such as -CC, -CXC, -CCX, -CCXX, -CCXXX, or CXXX
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
substrate are Rab3 and Rab4
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme crucial for membrane association and function of Rab proteins in intracellular vesicular trafficking
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
substrate are three tomato cDNAs endcoding Rab-like proteins: LeRab1A, B and C with mutant and wild-type prenylation motif, LeRab1B is the best substrate for the plant enzyme, but LeRab1A is the best substrate for yeast enzyme
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme catalyses the transfer of two 20-carbon geranylgeranyl groups from geranylgeranyl diphosphate onto C-terminal cysteine residues of Rab-proteins
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme catalyses the transfer of two 20-carbon geranylgeranyl groups from geranylgeranyl diphosphate onto C-terminal cysteine residues of Rab-proteins
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
this posttranslational modification is essential for the biological activity of Rab proteins
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme crucial for membrane association and function of Rab proteins in intracellular vesicular trafficking
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme attaches geranylgeranyl groups to two C-terminal cysteines in Ras-related GTPases of a single family, the Rab family, Ypt/Sec4 in lower eukaryotes, that terminate in XXCC, XCXC and CCXX motifs, reaction only if Rab is bound to a carrier protein termed Rab escort protein, REP
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme attaches geranylgeranyl groups to two C-terminal cysteines in Ras-related GTPases of a single family, the Rab family, Ypt/Sec4 in lower eukaryotes, that terminate in XXCC, XCXC and CCXX motifs, reaction only if Rab is bound to a carrier protein termed Rab escort protein, REP
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme attaches geranylgeranyl groups to two C-terminal cysteines in Ras-related GTPases of a single family, the Rab family, Ypt/Sec4 in lower eukaryotes, that terminate in XXCC, XCXC and CCXX motifs, reaction only if Rab is bound to a carrier protein termed Rab escort protein, REP
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
Rab protein forms a stable complex with Rab escort protein, REP
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
Rab protein forms a stable complex with Rab escort protein, REP
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
substrate are three tomato cDNAs endcoding Rab-like proteins: LeRab1A, B and C with mutant and wild-type prenylation motif, LeRab1B is the best substrate for the plant enzyme, but LeRab1A is the best substrate for yeast enzyme
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme attaches geranylgeranyl groups to two C-terminal cysteines in Ras-related GTPases of a single family, the Rab family, Ypt/Sec4 in lower eukaryotes, that terminate in XXCC, XCXC and CCXX motifs, reaction only if Rab is bound to a carrier protein termed Rab escort protein, REP
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
substrate are three tomato cDNAs endcoding Rab-like proteins: LeRab1A, B and C with mutant and wild-type prenylation motif, LeRab1B is the best substrate for the plant enzyme, but LeRab1A is the best substrate for yeast enzyme
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
-
intracellular vesicular trafficking is regulated by Rab proteins, small GTPases that require posttranslational geranylgeranylation for biological activity, which is catalyzed by the enzyme, a Rab geranylgeranyl transferase in complex with the Rab escort protein, REP, overview
-
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
-
intracellular vesicular trafficking is regulated by Rab proteins, small GTPases that require posttranslational geranylgeranylation for biological activity, which is catalyzed by the enzyme, a Rab geranylgeranyl transferase together with the Rab escort protein, REP, overview
-
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
-
with recombinantly expressed His6-tagged Saccharomyces cerevisiae Rab GTPase Ypt1 and Nicotiana tabacum NtaRabA1a in vitro substrates, overview
-
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
-
Rab proteins are members of the Ras superfamily of GTPases and are key regulators of intracellular vesicular transport, they undergo a cycle of GTPase activity, and this activity is interconnected to a cycle of reversible attachment to membranes. This cycle is mediated by geranylgeranylation of usually two C-terminal cysteines, which in turn is effected by Rab geranylgeranyltransferase in concert with Rab escort protein REP, Rab prenylation, delivery to membranes and the GTPase cycle, overview, alternative and classical pathways, overview
-
-
?
geranylgeranyl diphosphate + Ypt1p
?
-
yeast enzyme catalyses the prenylation of Ypt1p in the presence of an escort protein, Msi4p
-
-
?
geranylgeranyl diphosphate + Ypt1p
?
-
yeast enzyme catalyses the prenylation of Ypt1p in the presence of an escort protein, Msi4p
-
-
?
additional information
?
-
-
the enzyme is complexed with the Rab escort protein, REP, recombinant Arabidopsis thaliana REP interacts with yeast 6His-Ypt1, tobacco 6His-RabA1a, and Arabidopsis RabA2a in vitro preferring the GDP-bound form of the latter, overview, enzyme activity with different REPs, wild-type and mutant REPs, and involved REP residues, overview
-
-
?
additional information
?
-
Arabidopsis thaliana Rab geranylgeranyltransferases demonstrate redundancy and broad substrate specificity in vitro, comparisons of isozymes and subunits, respectively, overview. RGTB1 and RGTB2 are biochemically redundant Rab-GGT alpha-subunits in Arabidopsis, whereas RGTA1 is the active alpha subunit, while RGTA2 is not. Rab-GGT alpha-subunits in Arabidopsis partner with putative beta-subunits as functional Rab-GGTs. The two subunits in all of the four combinations physically interact with each other, interaction analysis
-
-
?
additional information
?
-
Arabidopsis thaliana Rab geranylgeranyltransferases demonstrate redundancy and broad substrate specificity in vitro, comparisons of isozymes and subunits, respectively, overview. RGTB1 and RGTB2 are biochemically redundant Rab-GGT alpha-subunits in Arabidopsis, whereas RGTA1 is the active alpha subunit, while RGTA2 is not. Rab-GGT alpha-subunits in Arabidopsis partner with putative beta-subunits as functional Rab-GGTs. The two subunits in all of the four combinations physically interact with each other, interaction analysis
-
-
?
additional information
?
-
Arabidopsis thaliana Rab geranylgeranyltransferases demonstrate redundancy and broad substrate specificity in vitro, comparisons of isozymes and subunits, respectively, overview. RGTB1 and RGTB2 are biochemically redundant Rab-GGT alpha-subunits in Arabidopsis, whereas RGTA1 is the active alpha subunit, while RGTA2 is not. Rab-GGT alpha-subunits in Arabidopsis partner with putative beta-subunits as functional Rab-GGTs. The two subunits in all of the four combinations physically interact with each other, interaction analysis
-
-
?
additional information
?
-
Arabidopsis thaliana Rab geranylgeranyltransferases demonstrate redundancy and broad substrate specificity in vitro, comparisons of isozymes and subunits, respectively, overview. RGTB1 and RGTB2 are biochemically redundant Rab-GGT alpha-subunits in Arabidopsis, whereas RGTA1 is the active alpha subunit, while RGTA2 is not. Rab-GGT alpha-subunits in Arabidopsis partner with putative beta-subunits as functional Rab-GGTs. The two subunits in all of the four combinations physically interact with each other, interaction analysis
-
-
?
additional information
?
-
-
Arabidopsis thaliana Rab geranylgeranyltransferases demonstrate redundancy and broad substrate specificity in vitro, comparisons of isozymes and subunits, respectively, overview. RGTB1 and RGTB2 are biochemically redundant Rab-GGT alpha-subunits in Arabidopsis, whereas RGTA1 is the active alpha subunit, while RGTA2 is not. Rab-GGT alpha-subunits in Arabidopsis partner with putative beta-subunits as functional Rab-GGTs. The two subunits in all of the four combinations physically interact with each other, interaction analysis
-
-
?
additional information
?
-
-
reduction in RabGGT function can be sufficient to induce cancer cell lines to undergo p53-independent apoptosis
-
-
?
additional information
?
-
the C-terminal cysteines of Rab3a contribute to the interaction with enzyme
-
-
?
additional information
?
-
-
reduction in RabGGT function can be sufficient to induce cancer cell lines to undergo p53-independent apoptosis
-
-
?
additional information
?
-
-
unlike the other prenyltransferases, farnesyl-transferase and geranylgeranyl-transferase I (GGTaseI), RabGGTase does not rely on a consensus sequence such as the CAAX box, but instead has delegated substrate recognition to a third protein, the Rab escort protein (REP)
-
-
?
additional information
?
-
-
farnesyl diphosphate and geranylgeranyl diphosphate bind to enzyme with very similar rate constant, but the binding mechanism of farnesyl diphosphate differs from that of geranylgeranyl diphosphate, shortening of the isoprenoid chain leads to a drastic decreases in affinity
-
-
?
additional information
?
-
-
the affinity of the mono-prenylated Rab7/REP-1 complex is very close to that observed for double prenylated Rab7/REP-1 complex binding to enzyme
-
-
?
additional information
?
-
-
yeast enzyme binding of farnesyl diphosphate is as weaker as of geranylgeranyl diphosphate, the length of isoprenoids has an influence on their affinity for enzyme, but unlike the mammalian enzyme, yeast enzyme binds prenylated and unprenylated Yptp/Mrs6p complex with similar affinities, phosphoisoprenoids do not influence the affinity of Mrs6p for yeast enzyme
-
-
?
additional information
?
-
-
RabGGTase, which prenylates more than 60 members of the Rab GTPase family, can act on its protein substrates only when they are complexed to an additional factor termed REP, Rab escort protein
-
-
?
additional information
?
-
-
yeast enzyme binding of farnesyl diphosphate is as weaker as of geranylgeranyl diphosphate, the length of isoprenoids has an influence on their affinity for enzyme, but unlike the mammalian enzyme, yeast enzyme binds prenylated and unprenylated Yptp/Mrs6p complex with similar affinities, phosphoisoprenoids do not influence the affinity of Mrs6p for yeast enzyme
-
-
?
additional information
?
-
-
structural and mechanistic basis for recycling of Rab proteins between membrane compartments, overview
-
-
?
additional information
?
-
-
the enzyme is complexed with the Rab escort protein, REP, which is essential for enzyme activity, binary complex structure, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
geranylgeranyl diphosphate + Arabidopsis thaliana RAB-ATa protein
S-geranylgeranyl-RAB GTPase + diphosphate
-
homozygous insertion mutants (rgtb1-1 and rgtb1-2) of the major beta-subunit of Arabidopsis enzyme (RGTB1) lead to reduced enzyme activity (about 25%), 50 mM phosphate buffer, pH 7.6, 10 mM MgCl2, 5 mM DTT, 0.5 microM tritium-labelled all trans-geranylgeranyl pyrophosphate, 4 microg recombinant Arabidopsis thaliana RAB-A2a protein, 32°C, 40 min
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
geranylgeranyl diphosphate + Rab
S-geranylgeranyl-Rab + diphosphate
-
His6- and gluthathione S-transferase-tagged Rab proteins such as canine Rab1a, human Rab27a, Rab5a, Rab18, Rab6a, Rab13, and mouse Rab23
-
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
additional information
?
-
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
the Rab protein Rab8-GTPase, which end with a Cys-Val-Leu-Leu motif able to serve as a substrate for either geranylgeranyl transferase I and II, but modified predominantly by either geranylgeranyl transferase II in vivo
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
the enzyme catalyzes posttranslational modification of proteins, the farnesyl moieties attached to the substrates are directly involved in protein-protein interactions as well as in protein-membrane interactions
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme crucial for membrane association and function of Rab proteins in intracellular vesicular trafficking
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
this posttranslational modification is essential for the biological activity of Rab proteins
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme crucial for membrane association and function of Rab proteins in intracellular vesicular trafficking
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins
-
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
-
intracellular vesicular trafficking is regulated by Rab proteins, small GTPases that require posttranslational geranylgeranylation for biological activity, which is catalyzed by the enzyme, a Rab geranylgeranyl transferase in complex with the Rab escort protein, REP, overview
-
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
-
intracellular vesicular trafficking is regulated by Rab proteins, small GTPases that require posttranslational geranylgeranylation for biological activity, which is catalyzed by the enzyme, a Rab geranylgeranyl transferase together with the Rab escort protein, REP, overview
-
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
-
Rab proteins are members of the Ras superfamily of GTPases and are key regulators of intracellular vesicular transport, they undergo a cycle of GTPase activity, and this activity is interconnected to a cycle of reversible attachment to membranes. This cycle is mediated by geranylgeranylation of usually two C-terminal cysteines, which in turn is effected by Rab geranylgeranyltransferase in concert with Rab escort protein REP, Rab prenylation, delivery to membranes and the GTPase cycle, overview, alternative and classical pathways, overview
-
-
?
additional information
?
-
-
reduction in RabGGT function can be sufficient to induce cancer cell lines to undergo p53-independent apoptosis
-
-
?
additional information
?
-
-
reduction in RabGGT function can be sufficient to induce cancer cell lines to undergo p53-independent apoptosis
-
-
?
additional information
?
-
-
unlike the other prenyltransferases, farnesyl-transferase and geranylgeranyl-transferase I (GGTaseI), RabGGTase does not rely on a consensus sequence such as the CAAX box, but instead has delegated substrate recognition to a third protein, the Rab escort protein (REP)
-
-
?
additional information
?
-
-
RabGGTase, which prenylates more than 60 members of the Rab GTPase family, can act on its protein substrates only when they are complexed to an additional factor termed REP, Rab escort protein
-
-
?
additional information
?
-
-
structural and mechanistic basis for recycling of Rab proteins between membrane compartments, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2-[(1-geranylgeranyl)-1H-1,2,3-triazol-4-yl]ethane-1,1-diyl)bis(phosphonate)
-
compound is able to induce cytotoxicity in human myeloma cells, IC50 value 1 mM
(2R,3R,4S,5R)-2-(3,4-dichlorophenyl)-4-(hexylsulfanyl)-1-[(4-methylphenyl)sulfonyl]-5-propylpyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-2-(4-bromophenyl)-1-[(4-methylphenyl)sulfonyl]-4-(pentylsulfanyl)-5-propylpyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-2-(4-bromophenyl)-4-(hexylsulfanyl)-1-[(4-methylphenyl)sulfonyl]-5-propylpyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-2-(4-bromophenyl)-4-[(4-methoxyphenyl)sulfanyl]-1-[(4-methylphenyl)sulfonyl]-5-propylpyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-2-(4-bromophenyl)-5-ethyl-4-(hexylsulfanyl)-1-[(4-methylphenyl)sulfonyl]pyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-2-(4-bromophenyl)-5-hexyl-4-(hexylsulfanyl)-1-[(4-methylphenyl)sulfonyl]pyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-4-[(3-tert-butoxy-3-oxopropyl)sulfanyl]-2-(3-chlorophenyl)-5-(cyclopentylmethyl)-1-[(4-methylphenyl)sulfonyl]pyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-4-[(3-tert-butoxy-3-oxopropyl)sulfanyl]-2-(4-chlorophenyl)-1-[(4-chlorophenyl)sulfonyl]-5-(cyclopentylmethyl)pyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-4-[(3-tert-butoxy-3-oxopropyl)sulfanyl]-2-(4-chlorophenyl)-5-(cyclopentylmethyl)-1-(phenylsulfonyl)pyrrolidine-3-carboxylic acid
-
-
(2S,5S)-5-tert-butyl-2-(4-chlorophenyl)-1-[(2-methylphenyl)sulfonyl]-2,5-dihydro-1H-pyrrole-3-carboxylic acid
-
slight inhibition of RabGGTase at concentrations above 0.01 mM
2-(3-pyridinyl)-1-ethylidene-1,1-phosphonocarboxylic acid
-
causes rapid accumulation of unprenylated Rabs within the cytosol of osteoclasts and macrophages due to specific inhibition of Rab GGTase
2-(3-pyridinyl)-1-hydroxyethylidene-1,1-bisphosphonic acid
-
causes rapid accumulation of unprenylated Rabs within the cytosol of osteoclasts and macrophages due to specific inhibition of Rab GGTase
2-(3-pyridinyl)-1-hydroxyethylidene-1,1-phosphonocarboxylic acid
-
causes rapid accumulation of unprenylated Rabs within the cytosol of osteoclasts and macrophages due to specific inhibition of Rab GGTase
2-bromo-3-(3-pyridinyl)-2-phosphonopropionic acid
-
-
2-chloro-3-(3-pyridinyl)-2-phosphonopropionic acid
-
-
2-fluoro-3-(1-methyl-1H-imidazol-5-yl)-2-phosphonopropanoic acid
compound inhibits isoform Rab11A, but not Rap1A/Rap1B prenylation in HeLa cells
2-fluoro-3-(1H-imidazol-4(5)-yl)-2-phosphonopropanoic acid
compound inhibits isoform Rab11A, but not Rap1A/Rap1B prenylation in HeLa cells
2-fluoro-3-(3-pyridinyl)-2-phosphonopropionic acid
-
-
2-fluoro-3-(6-methylimidazo[1,2-a]pyridin-3-yl)-2-phosphonopropanoic acid
compound is an micromolar inhibitor of Rab11A prenylation, is inactive against Rap1A/Rap1B modification, and able to inhibit proliferation of HeLa cell line with IC50 value of 0.36 mM
2-fluoro-3-(6-phenylimidazo[1,2-a]pyridin-3-yl)-2-phosphonopropanoic acid
compound is an micromolar inhibitor of Rab11A prenylation, is inactive against Rap1A/Rap1B modification, and able to inhibit proliferation of HeLa cell line with IC50 value of 0.51 mM
2-hydroxy-2-phosphono-3-pyridin-3-yl-propionic acid
-
3-PEHPC, weak inhibitor, 100% activity remain with concentrations up to 1 microM inhibitor and substrate Rab1a, with 10 microM inhibitor about 60% activity remain, with 100 microM and more inhibitor the activity falls to 30% and below
2-hydroxy-3-imidazo[1,2-a]pyridin-3-yl-2-phosphonopropionic acid
-
(+)-3-IPEHPC, the (+)-enantiomer is selective towards the enzyme and more potent than the (-)-enantiomer, mixed type inhibitor with respect to geranylgeranyl diphosphate, uncompetitive inhibitor with respect to Rab substrate, 25fold more potent than 2-hydroxy-2-phosphono-3-pyridin-3-yl-propionic acid, with 1 microM inhibitor activity falls to about 50%, with 10 microM inhibitor and more activity falls below 20%
2-PEPC
-
i.e.3-PEPC, protein geranylgeranyltransferase-II is the major pharmacological target of the inhibitor
3-(1-methylpyridin-1-ium-3-yl)-2-phosphonopropanoate
-
i.e.NE1048 , protein geranylgeranyltransferase-II is the major pharmacological target of the inhibitor
3-(3-pyridinyl)-2-phosphonopropionic acid
-
-
3-(6-bromoimidazo[1,2-a]pyridin-3-yl)-2-fluoro-2-phosphonopropanoic acid
compound is an micromolar inhibitor of Rab11A prenylation, is inactive against Rap1A/Rap1B modification, and able to inhibit proliferation of HeLa cell line with IC50 value of 0.50 mM
3-(6-chloroimidazo[1,2-a]pyridin-3-yl)-2-fluoro-2-phosphonopropanoic acid
compound is an micromolar inhibitor of Rab11A prenylation, is inactive against Rap1A/Rap1B modification, and able to inhibit proliferation of HeLa cell line with IC50 value of 0.52 mM
3-PEHPC
-
i.e.3-PEHPC, protein geranylgeranyltransferase-II is the major pharmacological target of the inhibitor
3-PEPC
-
i.e.2-PEPC, protein geranylgeranyltransferase-II is the major pharmacological target of the inhibitor
3-pyridinyl ethylidene hydroxyl phosphonocarboxylate
-
previously known as NE10790
KCl
-
50% inhibition at 100 mM
methyl N-undecanoyl-L-tyrosyl-L-histidyl-L-tyrosinate
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide)
N-([[2-(benzyloxy)benzyl]oxy]carbonyl)-D-histidyl-L-tyrosyl-L-phenylalanine
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini)
N-([[2-(benzyloxy)benzyl]oxy]carbonyl)-L-histidyl-L-tyrosyl-L-phenylalanine
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini)
N-butanoyl-L-histidyl-L-phenylalanyl-N-methyl-N-[2-(pyridin-2-yl)ethyl]-L-tyrosinamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide)
N-octanoyl-L-histidyl-L-phenylalanyl-N-methyl-N-[2-(pyridin-2-yl)ethyl]-L-tyrosinamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide)
N-pentadecanoyl-L-histidyl-L-phenylalanyl-N-methyl-N-[2-(pyridin-2-yl)ethyl]-L-tyrosinamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide)
N-undecanoyl-L-histidyl-L-histidyl-N-(4-aminobutyl)-L-tyrosinamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide)
N-undecanoyl-L-histidyl-L-histidyl-N-methyl-N-[2-(pyridin-2-yl)ethyl]-L-tyrosinamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide), not cytotoxic to COS-7 cells, fluorescence titration reveals competitive inhibition
N-undecanoyl-L-histidyl-L-phenylalanyl-N-methyl-N-[2-(pyridin-2-yl)ethyl]-L-tyrosinamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide), not cytotoxic to COS-7 cells, fluorescence titration reveals partial competitive inhibition which points to a different binding site
N-undecanoyl-L-histidyl-L-phenylalanyl-N-[2-(pyridin-2-yl)ethyl]-L-tyrosinamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide)
N-undecanoyl-L-tyrosyl-L-histidyl-N-(4-aminobutyl)-L-tyrosinamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide)
N-undecanoyl-L-tyrosyl-L-histidyl-N-methyl-N-[2-(pyridin-2-yl)ethyl]-L-tyrosinamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide), not cytotoxic to COS-7 cells, fluorescence titration reveals competitive inhibition
N-[(2,5-dimethyl-1,3-oxazol-4-yl)carbonyl]glycyl-L-phenylalanyl-1-trityl-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[(2,5-dimethyl-1,3-oxazol-4-yl)carbonyl]glycyl-L-phenylalanyl-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[(2-phenyl-1,3-oxazol-4-yl)carbonyl]-1-trityl-L-histidylglycyl-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[(2-phenyl-1,3-oxazol-4-yl)carbonyl]-1-trityl-L-histidylglycyl-L-phenylalanine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[(2-phenyl-1,3-oxazol-4-yl)carbonyl]-L-histidylglycyl-1-trityl-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus), not cytotoxic to COS-7 cells, fluorescence titration reveals competitive inhibition
N-[(2-phenyl-1,3-oxazol-4-yl)carbonyl]-L-histidylglycyl-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[(2-phenyl-1,3-oxazol-4-yl)carbonyl]glycyl-L-phenylalanyl-1-(tert-butoxycarbonyl)-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[(2-phenyl-1,3-oxazol-4-yl)carbonyl]glycyl-L-phenylalanyl-1-benzyl-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[(2-phenyl-1,3-oxazol-4-yl)carbonyl]glycyl-L-phenylalanyl-1-trityl-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[(2-phenyl-1,3-oxazol-4-yl)carbonyl]glycyl-L-phenylalanyl-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[(2-phenyl-1,3-oxazol-4-yl)carbonyl]histidylglycyl-L-phenylalanine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[(2E)-3-(biphenyl-4-yl)prop-2-enoyl]-D-histidyl-L-tyrosyl-L-tyrosine
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini)
N-[(2E)-3-[2-[(1Z)-pent-1-en-1-yl]phenyl]prop-2-enoyl]-D-histidyl-L-tyrosyl-D-phenylalanine
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini)
N-[(benzyloxy)carbonyl]-D-tyrosyl-L-phenylalanyl-L-tyrosine
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), fluorescence titration reveals competitive inhibition
N-[(benzyloxy)carbonyl]-L-histidyl-N-methyl-L-phenylalanyl-L-tyrosine
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), fluorescence titration reveals competitive inhibition
N-[(benzyloxy)carbonyl]-L-histidyl-N-methyl-L-phenylalanyl-N-hydroxy-D-tyrosinamide
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini)
N-[(benzyloxy)carbonyl]-L-histidyl-N-methyl-L-phenylalanyl-N-hydroxy-L-tryptophanamide
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), not cytotoxic to COS-7 cells
N-[(benzyloxy)carbonyl]-L-histidyl-N-methyl-L-phenylalanyl-N-hydroxy-L-tyrosinamide
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), not cytotoxic to COS-7 cells
N-[3-(4-pentylphenyl)propanoyl]-D-histidyl-N-methyl-L-phenylalanyl-L-phenylalanine
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini)
N-[3-(4-pentylphenyl)propanoyl]-D-tyrosyl-L-tyrosyl-L-phenylalanine
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini)
N-[4-(undecyloxy)benzoyl]-L-histidyl-L-histidyl-N-(4-aminobutyl)-L-histidinamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide)
N-[4-(undecyloxy)benzoyl]-L-histidyl-L-histidyl-N-methyl-N-[2-(pyridin-2-yl)ethyl]-L-histidinamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide)
N-[4-(undecyloxy)benzoyl]-L-histidyl-L-tyrosyl-N-[3-(1H-imidazol-1-yl)propyl]-L-phenylalaninamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide)
N-[4-(undecyloxy)benzoyl]-L-tyrosyl-L-tyrosyl-N-(4-aminobutyl)-L-tyrosinamide
-
class III inhibitors (comprising a lipophilic N-terminus and an amine or N-heterocycle containing a C-terminal amide)
N-[[2-(pyridin-3-yl)-1,3-thiazol-4-yl]carbonyl]glycyl-L-phenylalanyl-1-trityl-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[[2-(pyridin-3-yl)-1,3-thiazol-4-yl]carbonyl]glycyl-L-phenylalanyl-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[[2-(thiophen-2-yl)-1,3-thiazol-4-yl]carbonyl]glycyl-L-phenylalanyl-1-trityl-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
N-[[2-(thiophen-2-yl)-1,3-thiazol-4-yl]carbonyl]glycyl-L-phenylalanyl-L-histidine
-
class II inhibitors (combining a heterocyclic ring system at the N-terminus with a free carboxylate at the C-terminus)
NaCl
-
50% inhibition at 100 mM
NaOAc
-
50% inhibition at 100 mM
NE10790
-
a weak bisphosphonate inhibitor
Zn2+
-
in the presence of saturating concentrations of MgCl2 100% inhibition at 0.2 mM
Zn2+
-
at concentrations above 0.01 mM
additional information
-
peptidic library based on the farnesyl transferase inhibitor pepticinnamin E, a natural tripeptide from Streptomyces OH-4652
-
additional information
-
perillyl alcohol inhibits insulin induced activation of enzyme, but not GGTI-298 and alpha-hxdroxyfarnesylphosphonic acid, PD 98056 inhibits the ability of insulin to increase the amount of geranylgeranylated Rab3 and Rab4 proteins
-
additional information
-
protein geranylgeranyltransferase-II is the major pharmacological target of phosphonocarboxylate inhibitors. Analysis of several different phosphonocarboxylate drugs demonstrates a very good correlation between the ability of these drugs to inhibit the enzyme with their ability to reduce macrophage cell viability and induce apoptosis
-
additional information
-
plant enzyme is inhibited by mutant Rab lacking a prenylation consence sequence
-
additional information
-
plant enzyme is inhibited by mutant Rab lacking a prenylation consence sequence
-
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Acquired Immunodeficiency Syndrome
Rab11a regulates Syntaxin 3 localization and microvillus assembly in enterocytes.
Barrett Esophagus
Rab11a immunohistochemical analysis does not distinguish indefinite, low-, and high-grade dysplasia in Barrett esophagus.
Blindness
Choroideremia: molecular mechanisms and development of AAV gene therapy.
Breast Neoplasms
MicroRNA-320a inhibits proliferation and invasion of breast cancer cells by targeting RAB11A.
Breast Neoplasms
The Lipid Kinase PI4KIII? Is Highly Expressed in Breast Tumors and Activates Akt in Cooperation with Rab11a.
Breast Neoplasms
Tumor-suppressive microRNA-452 inhibits migration and invasion of breast cancer cells by directly targeting RAB11A.
Carcinogenesis
c-Fos-dependent induction of the small ras-related GTPase Rab11a in skin carcinogenesis.
Carcinogenesis
Influenza Virus Induces Cholesterol-Enriched Endocytic Recycling Compartments for Budozone Formation via Cell Cycle-Independent Centrosome Maturation.
Carcinogenesis
The Lipid Kinase PI4KIII? Is Highly Expressed in Breast Tumors and Activates Akt in Cooperation with Rab11a.
Carcinoma
Differential gene expression between squamous cell carcinoma of esophageus and its normal epithelium; altered pattern of mal, akr1c2, and rab11a expression.
Carcinoma
Rab11a immunohistochemical analysis does not distinguish indefinite, low-, and high-grade dysplasia in Barrett esophagus.
Carcinoma
Studies of the mouse Rab geranylgeranyl transferase beta subunit: gene structure, expression and regulation.
Carcinoma
Synthesis of the 6-Substituted Imidazo[1,2-a]Pyridine-3-yl-2- Phosphonopropionic Acids as Potential Inhibitors of Rab Geranylgeranyl Transferase.
Carcinoma, Ductal
Rab11a differentially modulates epidermal growth factor-induced proliferation and motility in immortal breast cells.
Carcinoma, Hepatocellular
Rab11a regulates MMP2 expression by activating the PI3K/AKT pathway in human hepatocellular carcinoma cells.
Carcinoma, Intraductal, Noninfiltrating
Rab11a differentially modulates epidermal growth factor-induced proliferation and motility in immortal breast cells.
Carcinoma, Non-Small-Cell Lung
Rab11a promotes proliferation and invasion through regulation of YAP in non-small cell lung cancer.
Carcinoma, Squamous Cell
Differential gene expression between squamous cell carcinoma of esophageus and its normal epithelium; altered pattern of mal, akr1c2, and rab11a expression.
Cholestasis
Hormonal Modulation of Hepatic cAMP Prevents Estradiol 17?-D-Glucuronide-Induced Cholestasis in Perfused Rat Liver.
Choroideremia
cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein.
Choroideremia
Choroideremia gene testing.
Choroideremia
Choroideremia: molecular mechanisms and development of AAV gene therapy.
Choroideremia
Comprehensive mutation analysis (20 families) of the choroideremia gene reveals a missense variant that prevents the binding of REP1 with Rab geranylgeranyl transferase.
Choroideremia
Deficient geranylgeranylation of Ram/Rab27 in choroideremia.
Choroideremia
Identification of yeast component A: reconstitution of the geranylgeranyltransferase that modifies Ypt1p and Sec4p.
Choroideremia
Purification of component A of Rab geranylgeranyl transferase: possible identity with the choroideremia gene product.
Choroideremia
Retinal degeneration in choroideremia: deficiency of rab geranylgeranyl transferase.
Choroideremia
[Structure and properties of Rab proteins]
Crohn Disease
TLR sorting by Rab11 endosomes maintains intestinal epithelial-microbial homeostasis.
Cysts
Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization.
Cysts
Tankyrase regulates epithelial lumen formation via suppression of Rab11 GEFs.
Cytomegalovirus Infections
Myosin Vb and Rab11a regulate phosphorylation of ezrin in enterocytes.
Cytomegalovirus Infections
Myosin Vb uncoupling from RAB8A and RAB11A elicits microvillus inclusion disease.
Diabetic Retinopathy
Choroideremia: molecular mechanisms and development of AAV gene therapy.
Enteritis
1,25-Dihydroxyvitamin D3 and dietary vitamin D reduce inflammation in mice lacking intestinal epithelial cell Rab11a.
Esophageal Neoplasms
RAB11A mediates the proliferation and motility of esophageal cancer cells via WNT signaling pathway.
Genetic Diseases, Inborn
Prenylation of Rab GTPases: molecular mechanisms and involvement in genetic disease.
Genetic Diseases, Inborn
Rab GTPases, intracellular traffic and disease.
Genetic Diseases, Inborn
[Structure and properties of Rab proteins]
Hermanski-Pudlak Syndrome
[Structure and properties of Rab proteins]
Infections
Enteropathogenic Escherichia coli remodels host endosomes to promote endocytic turnover and breakdown of surface polarity.
Infections
Expression of rab11a N124I in gastric parietal cells inhibits stimulatory recruitment of the H+-K+-ATPase.
Infections
Intracellular Colocalization of Influenza Viral RNA and Rab11A Is Dependent upon Microtubule Filaments.
Infections
Proteomic and metabolomic responses in hepatopancreas of whiteleg shrimp Litopenaeus vannamei infected by microsporidian Enterocytozoon hepatopenaei.
Infections
Quantitative live cell imaging reveals influenza virus manipulation of Rab11A transport through reduced dynein association.
Infections
Rab11a is required for porcine reproductive and respiratory syndrome virus induced autophagy to promote viral replication.
Infections
Rab11a mediates cell-cell spread and reassortment of influenza A virus genomes via tunneling nanotubes.
Infertility
Rab11a drives adhesion molecules to the surface of endometrial epithelial cells.
Influenza, Human
Activation of Dendritic Cells Alters the Mechanism of MHC Class II Antigen Presentation to CD4 T Cells.
Influenza, Human
Host factor Rab11a is critical for efficient assembly of influenza A virus genomic segments.
Influenza, Human
Influenza A Virus NS1 Protein Suppresses JNK1-Dependent Autophagosome Formation Mediated by Rab11a Recycling Endosomes.
Influenza, Human
Influenza Virus Induces Cholesterol-Enriched Endocytic Recycling Compartments for Budozone Formation via Cell Cycle-Independent Centrosome Maturation.
Influenza, Human
Intracellular Colocalization of Influenza Viral RNA and Rab11A Is Dependent upon Microtubule Filaments.
Influenza, Human
Quantitative live cell imaging reveals influenza virus manipulation of Rab11A transport through reduced dynein association.
Influenza, Human
RAB11A is essential for transport of the influenza virus genome to the plasma membrane.
Influenza, Human
Rab11a mediates cell-cell spread and reassortment of influenza A virus genomes via tunneling nanotubes.
Leber Congenital Amaurosis
Choroideremia: molecular mechanisms and development of AAV gene therapy.
Lung Injury
Inactivation of Rab11a GTPase in Macrophages Facilitates Phagocytosis of Apoptotic Neutrophils.
Lung Neoplasms
Rab11a promotes proliferation and invasion through regulation of YAP in non-small cell lung cancer.
Malaria
Bioaffinity Mass Spectrometry Screening.
Malaria
Zygote morphogenesis but not the establishment of cell polarity in Plasmodium berghei is controlled by the small GTPase, RAB11A.
Neoplasm Metastasis
Rab11a Is Overexpressed in Gastric Cancer and Regulates FAK/AKT Signaling.
Neoplasms
Chemical genetics identifies Rab geranylgeranyl transferase as an apoptotic target of farnesyl transferase inhibitors.
Neoplasms
Design, synthesis, and characterization of peptide-based rab geranylgeranyl transferase inhibitors.
Neoplasms
Extracellular vesicles: eat glutamine and spit acidic bubbles.
Neoplasms
Glutamine deprivation alters the origin and function of cancer cell exosomes.
Neoplasms
Identification of Pan-Cancer Prognostic Biomarkers Through Integration of Multi-Omics Data.
Neoplasms
Identification of the Privileged Position in the Imidazo[1,2-a]pyridine Ring of Phosphonocarboxylates for Development of Rab Geranylgeranyl Transferase (RGGT) Inhibitors.
Neoplasms
MicroRNA-320a inhibits proliferation and invasion of breast cancer cells by targeting RAB11A.
Neoplasms
MiR-150 Inhibits Cell Growth In Vitro and In Vivo by Restraining the RAB11A/WNT/?-Catenin Pathway in Thyroid Cancer.
Neoplasms
Neoplastic reprogramming of patient-derived adipose stem cells by prostate cancer cell-associated exosomes.
Neoplasms
Psoromic acid is a selective and covalent Rab-prenylation inhibitor targeting autoinhibited RabGGTase.
Neoplasms
Rab11a differentially modulates epidermal growth factor-induced proliferation and motility in immortal breast cells.
Neoplasms
Rab11a Is Overexpressed in Gastric Cancer and Regulates FAK/AKT Signaling.
Neoplasms
RAB11A mediates the proliferation and motility of esophageal cancer cells via WNT signaling pathway.
Neoplasms
Rab11a promotes proliferation and invasion through regulation of YAP in non-small cell lung cancer.
Neoplasms
Rab11a regulates MMP2 expression by activating the PI3K/AKT pathway in human hepatocellular carcinoma cells.
Neoplasms
Rab11a sustains GSK3?/Wnt/?-catenin signaling to enhance cancer progression in pancreatic cancer.
Neoplasms
RAB11A-mediated YAP localization to adherens and tight junctions is essential for colonic epithelial integrity.
Neoplasms
Recycling Endosomes in Mature Epithelia Restrain Tumorigenic Signaling.
Neoplasms
Searching for non-RET molecular alterations in medullary thyroid carcinoma: expression analysis by mRNA differential display.
Neoplasms
Synthesis of a fluorescent analogue of geranylgeranyl pyrophosphate and its use in a high-throughput fluorometric assay for Rab geranylgeranyltransferase.
Neoplasms
Tumor-suppressive microRNA-452 inhibits migration and invasion of breast cancer cells by directly targeting RAB11A.
Osteoporosis
Psoromic acid is a selective and covalent Rab-prenylation inhibitor targeting autoinhibited RabGGTase.
Pancreatic Neoplasms
Rab11a sustains GSK3?/Wnt/?-catenin signaling to enhance cancer progression in pancreatic cancer.
Porcine Reproductive and Respiratory Syndrome
Rab11a is required for porcine reproductive and respiratory syndrome virus induced autophagy to promote viral replication.
protein geranylgeranyltransferase type ii deficiency
Host factor Rab11a is critical for efficient assembly of influenza A virus genomic segments.
protein geranylgeranyltransferase type ii deficiency
Rab11a regulates Syntaxin 3 localization and microvillus assembly in enterocytes.
Retinal Degeneration
Identification of yeast component A: reconstitution of the geranylgeranyltransferase that modifies Ypt1p and Sec4p.
Retinal Degeneration
Nucleotide bound to rab11a controls localization in rod cells but not interaction with rhodopsin.
Retinal Degeneration
Retinal degeneration in choroideremia: deficiency of rab geranylgeranyl transferase.
Retinal Diseases
Choroideremia: molecular mechanisms and development of AAV gene therapy.
Sepsis
Rab11a Mediates Vascular Endothelial-Cadherin Recycling and Controls Endothelial Barrier Function.
Skin Neoplasms
c-Fos-dependent induction of the small ras-related GTPase Rab11a in skin carcinogenesis.
Skin Neoplasms
Synthesis and characterization of novel phosphonocarboxylate inhibitors of RGGT.
Starvation
The RAB11A-Positive Compartment Is a Primary Platform for Autophagosome Assembly Mediated by WIPI2 Recognition of PI3P-RAB11A.
Stomach Neoplasms
Rab11a Is Overexpressed in Gastric Cancer and Regulates FAK/AKT Signaling.
Thrombocytosis
Cell-specific abnormal prenylation of Rab proteins in platelets and melanocytes of the gunmetal mouse.
Thrombocytosis
Rab geranylgeranyl transferase alpha mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis.
Virus Diseases
Influenza Virus Induces Cholesterol-Enriched Endocytic Recycling Compartments for Budozone Formation via Cell Cycle-Independent Centrosome Maturation.
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0.1
(2-[(1-geranylgeranyl)-1H-1,2,3-triazol-4-yl]ethane-1,1-diyl)bis(phosphonate)
Homo sapiens
-
temperature not specified in the publication, pH not specified in the publication
0.007
(2R,3R,4S,5R)-2-(3,4-dichlorophenyl)-4-(hexylsulfanyl)-1-[(4-methylphenyl)sulfonyl]-5-propylpyrrolidine-3-carboxylic acid
Rattus norvegicus
-
-
0.0036
(2R,3R,4S,5R)-2-(4-bromophenyl)-1-[(4-methylphenyl)sulfonyl]-4-(pentylsulfanyl)-5-propylpyrrolidine-3-carboxylic acid
Rattus norvegicus
-
-
0.0021
(2R,3R,4S,5R)-2-(4-bromophenyl)-4-(hexylsulfanyl)-1-[(4-methylphenyl)sulfonyl]-5-propylpyrrolidine-3-carboxylic acid
Rattus norvegicus
-
-
0.0045
(2R,3R,4S,5R)-2-(4-bromophenyl)-4-[(4-methoxyphenyl)sulfanyl]-1-[(4-methylphenyl)sulfonyl]-5-propylpyrrolidine-3-carboxylic acid
Rattus norvegicus
-
-
0.0048
(2R,3R,4S,5R)-2-(4-bromophenyl)-5-ethyl-4-(hexylsulfanyl)-1-[(4-methylphenyl)sulfonyl]pyrrolidine-3-carboxylic acid
Rattus norvegicus
-
-
0.0022
(2R,3R,4S,5R)-2-(4-bromophenyl)-5-hexyl-4-(hexylsulfanyl)-1-[(4-methylphenyl)sulfonyl]pyrrolidine-3-carboxylic acid
Rattus norvegicus
-
-
0.0047
(2R,3R,4S,5R)-4-[(3-tert-butoxy-3-oxopropyl)sulfanyl]-2-(3-chlorophenyl)-5-(cyclopentylmethyl)-1-[(4-methylphenyl)sulfonyl]pyrrolidine-3-carboxylic acid
Rattus norvegicus
-
-
0.0031
(2R,3R,4S,5R)-4-[(3-tert-butoxy-3-oxopropyl)sulfanyl]-2-(4-chlorophenyl)-1-[(4-chlorophenyl)sulfonyl]-5-(cyclopentylmethyl)pyrrolidine-3-carboxylic acid
Rattus norvegicus
-
-
0.007
(2R,3R,4S,5R)-4-[(3-tert-butoxy-3-oxopropyl)sulfanyl]-2-(4-chlorophenyl)-5-(cyclopentylmethyl)-1-(phenylsulfonyl)pyrrolidine-3-carboxylic acid
Rattus norvegicus
-
-
0.0177
2-bromo-3-(3-pyridinyl)-2-phosphonopropionic acid
Rattus norvegicus
-
-
0.0164
2-chloro-3-(3-pyridinyl)-2-phosphonopropionic acid
Rattus norvegicus
-
-
0.0163
2-fluoro-3-(3-pyridinyl)-2-phosphonopropionic acid
Rattus norvegicus
-
-
0.03185 - 0.86
2-hydroxy-2-phosphono-3-pyridin-3-yl-propionic acid
0.0353
3-(3-pyridinyl)-2-phosphonopropionic acid
Rattus norvegicus
-
-
0.0241
3-pyridinyl ethylidene hydroxyl phosphonocarboxylate
Rattus norvegicus
-
-
0.0156
N-([[2-(benzyloxy)benzyl]oxy]carbonyl)-D-histidyl-L-tyrosyl-L-phenylalanine
Homo sapiens
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), 9 microM (3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1) diphosphate, 3 microM Rab7, 3 microM Rab escort protein, 400 nM enzyme
0.0193
N-([[2-(benzyloxy)benzyl]oxy]carbonyl)-L-histidyl-L-tyrosyl-L-phenylalanine
Homo sapiens
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), 9 microM (3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1) diphosphate, 3 microM Rab7, 3 microM Rab escort protein, 400 nM enzyme
0.0227
N-[(2E)-3-(biphenyl-4-yl)prop-2-enoyl]-D-histidyl-L-tyrosyl-L-tyrosine
Homo sapiens
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), 9 microM (3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1) diphosphate, 3 microM Rab7, 3 microM Rab escort protein, 400 nM enzyme
0.0152
N-[(2E)-3-[2-[(1Z)-pent-1-en-1-yl]phenyl]prop-2-enoyl]-D-histidyl-L-tyrosyl-D-phenylalanine
Homo sapiens
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), 9 microM (3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1) diphosphate, 3 microM Rab7, 3 microM Rab escort protein, 400 nM enzyme
0.0041
N-[(benzyloxy)carbonyl]-D-tyrosyl-L-phenylalanyl-L-tyrosine
Homo sapiens
-
most potent of the class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), 9 microM (3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1) diphosphate, 3 microM Rab7, 3 microM Rab escort protein, 400 nM enzyme
0.0227
N-[(benzyloxy)carbonyl]-L-histidyl-N-methyl-L-phenylalanyl-L-tyrosine
Homo sapiens
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), 9 microM (3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1) diphosphate, 3 microM Rab7, 3 microM Rab escort protein, 400 nM enzyme
0.0136
N-[(benzyloxy)carbonyl]-L-histidyl-N-methyl-L-phenylalanyl-N-hydroxy-D-tyrosinamide
Homo sapiens
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), 9 microM (3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1) diphosphate, 3 microM Rab7, 3 microM Rab escort protein, 400 nM enzyme
0.0052
N-[(benzyloxy)carbonyl]-L-histidyl-N-methyl-L-phenylalanyl-N-hydroxy-L-tryptophanamide
Homo sapiens
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), 9 microM (3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1) diphosphate, 3 microM Rab7, 3 microM Rab escort protein, 400 nM enzyme
0.009
N-[(benzyloxy)carbonyl]-L-histidyl-N-methyl-L-phenylalanyl-N-hydroxy-L-tyrosinamide
Homo sapiens
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), 9 microM (3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1) diphosphate, 3 microM Rab7, 3 microM Rab escort protein, 400 nM enzyme
0.019
N-[3-(4-pentylphenyl)propanoyl]-D-histidyl-N-methyl-L-phenylalanyl-L-phenylalanine
Homo sapiens
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), 9 microM (3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1) diphosphate, 3 microM Rab7, 3 microM Rab escort protein, 400 nM enzyme
0.011
N-[3-(4-pentylphenyl)propanoyl]-D-tyrosyl-L-tyrosyl-L-phenylalanine
Homo sapiens
-
class I inhibitors (compounds possessing a free carboxylic or hydroxamic acid at the C-terminus and lipophilic N-termini), 9 microM (3,7,11-trimethyl-12-(7-nitrobenzo[1,2,5]oxadiazo-4-ylamino)-dodeca-2,6,19-trien-1) diphosphate, 3 microM Rab7, 3 microM Rab escort protein, 400 nM enzyme
additional information
additional information
-
0.03185
2-hydroxy-2-phosphono-3-pyridin-3-yl-propionic acid
Homo sapiens
-
50 mM sodium HEPES, pH 7.2, 5 mM MgCl2, 1 mM Nonidet P-40, 1 mM dithioerythritol, 6 microM tritium-labelled geranylgeranyl diphosphate, 4 microM Rab1a-CC (wild type), 2 microM Rab escort protein 1, 50 nM enzyme, 20 min, 37°C
0.03268
2-hydroxy-2-phosphono-3-pyridin-3-yl-propionic acid
Homo sapiens
-
50 mM sodium HEPES, pH 7.2, 5 mM MgCl2, 1 mM Nonidet P-40, 1 mM dithioerythritol, 6 microM tritium-labelled geranylgeranyl diphosphate, 4 microM Rab27a-CGC (wild type), 2 microM Rab escort protein 1, 50 nM enzyme, 20 min, 37°C
0.04347
2-hydroxy-2-phosphono-3-pyridin-3-yl-propionic acid
Homo sapiens
-
50 mM sodium HEPES, pH 7.2, 5 mM MgCl2, 1 mM Nonidet P-40, 1 mM dithioerythritol, 6 microM tritium-labelled geranylgeranyl diphosphate, 4 microM Rab5a-CCSN (wild type), 2 microM Rab escort protein 1, 50 nM enzyme, 20 min, 37°C
0.86
2-hydroxy-2-phosphono-3-pyridin-3-yl-propionic acid
Homo sapiens
-
50 mM sodium HEPES, pH 7.2, 5 mM MgCl2, 1 mM Nonidet P-40, 1 mM dithioerythritol, 6 microM tritium-labelled geranylgeranyl diphosphate, 4 microM Rab5a-CCVLL, 2 microM Rab escort protein 1, 50 nM enzyme, 20 min, 37°C
additional information
additional information
Homo sapiens
-
chemicals that cause an activity decrease of more than 70% at 100 microM are selected for inhibition studies
-
additional information
additional information
Homo sapiens
-
the inhibitory action of 2-hydroxy-2-phosphono-3-pyridin-3-yl-propionic acid with substrates Rab1a-CSC and Rab1a-CCS are not determined, and is not significant (IC50 > 2 mM) with the substrates Rab1a-CS, Rab1aSC, Rab27a-CVLS, Rab5a-CCQNI, Rab5a-CVLL, Rab13-CSLG (wild type), Rab18-CSVL (wild type), and Rab23-CSVP (wild type), and IC50 > 1.592 mM with Rab6a-CSC
-
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Casey, P.J.; Seabra, M.C.
Protein prenyltransferases
J. Biol. Chem.
271
5289-5292
1996
Saccharomyces cerevisiae
brenda
Wilson, A.L.; Erdman, R.A.; Castellano, F.; Maltese, W.A.
Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases
Biochem. J.
333
497-504
1998
Bos taurus
-
brenda
Seabra, M.C.; Goldstein, J.L.; Sudhof, T.C.; Brown, M.S.
Rab geranylgeranyl transferase. A multisubunit enzyme that prenylates GTP-binding proteins terminating in Cys-X-Cys or Cys-Cys
J. Biol. Chem.
267
14497-14503
1992
Rattus norvegicus
brenda
Farnsworth, C.C.; Seabra, M.C.; Ericsson, L.H.; Gelb, M.H.; Glomset, J.A.
Rab geranylgeranyl transferase catalyses the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A
Proc. Natl. Acad. Sci. USA
91
11963-11967
1994
Rattus norvegicus
brenda
Zhang, H.; Seabra, M.C.; Deisenhofer, J.
Crystal structure of Rab geranylgeranyltransferase at 2.0 resolution
Structure Fold. Des.
8
241-251
2000
Rattus norvegicus
brenda
Thom, N.H.; Iakovenko, A.; Owen, D.; Scheidig, A.S.; Waldmann, H.; Goody, R.S.; Alexandrov, K.
Phosphoisoprenoid binding specificity of geranylgeranyltransferase type II
Biochemistry
39
12043-12052
2000
Rattus norvegicus
brenda
Thom, N.H.; Niculae, A.; Goody, R.S.; Alexandrov, K.
Double prenylation by RabGGTase can proceed without dissociation of the mono-prenylated intermediate
J. Biol. Chem.
276
48631-48636
2001
Rattus norvegicus
brenda
Thom, N.H.; Iakovenko, A.; Kalinin, A.; Waldmann, H.; Goody, R.S.; Alexandrov, K.
Allosteric regulation of substrate binding and product release in geranylgeranyltransferase type II
Biochemistry
40
268-274
2001
Rattus norvegicus
brenda
Kalinin, A.; Thom, N.H.; Iakovenko, A.; Heinemann, I.; Rostkova, E.; Constantinescu, A.T.; Alexandrov, K.
Expression of mammalian geranylgeranyltransferase type-II in Escherichia coli and its application for in vitro prenylation of Rab proteins
Protein Expr. Purif.
22
84-91
2001
Rattus norvegicus
brenda
Rak, A.; Niculae, A.; Kalinin, A.; Thom, N.H.; Sidorovitch, V.; Goody, R.S.; Alexandrov, K.
In vitro assembly, purification, and crystallization of the Rab geranylgeranyl transferase:substrate complex
Protein Expr. Purif.
25
23-30
2002
Rattus norvegicus
brenda
Dursina, B.; Thom, N.H.; Sidorovitch, V.; Niculae, A.; Iakovenko, A.; Rak, A.; Albert, S.; Ceacareanu, A.C.; Kolling, R.; Herrmann, C.; Goody, R.S.; Alexandrov, K.
Interaction of yeast Rab geranylgeranyl transferase with its protein and lipid substrates
Biochemistry
41
6805-6816
2002
Saccharomyces cerevisiae, Rattus norvegicus
brenda
Pylypenko, O.; Rak, A.; Reents, R.; Niculae, A.; Sidorovitch, V.; Cioaca, M.D.; Bessolitsyna, E.; Thoma, N.H.; Waldmann, H.; Schlichting, I.; Goody, R.S.; Alexandrov, K.
Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase
Mol. Cell
11
483-494
2003
Rattus norvegicus
brenda
Johannes, L.; Perez, F.; Laran-Chich, M.P.; Henry, J.P.; Darchen, F.
Characterization of the interaction of the monomeric GTP-binding protein Rab3a with geranylgeranyl transferase II
Eur. J. Biochem.
239
362-368
1996
Rattus norvegicus, Homo sapiens (P53611)
brenda
Goalstone, M.L.; Leitner, J.W.; Golovchenko, I.; Stjernholm, M.R.; Cormont, M.; Le Marchand-Brustel, Y.; Draznin, B.
Insulin promotes phosphorylation and activation of geranylgeranyltransferase II. Studies with geranylgeranylation of rab-3 and rab-4
J. Biol. Chem.
274
2880-2884
1999
Mus musculus
brenda
Loraine, A.E.; Yalovsky, S.; Fabry, S.; Gruissen, W.
Tomato Rab1A homologs as molecular tools for studying Rab geranylgeranyl transferase in plant cells
Plant Physiol.
110
1337-1347
1996
Saccharomyces cerevisiae, Solanum lycopersicum, Nicotiana tabacum
brenda
Witter, D.J.; Poulter, C.D.
Yeast geranylgeranyltransferase type-II: steady state kinetic studies of the recombinant enzyme
Biochemistry
35
10454-10463
1996
Saccharomyces cerevisiae, Saccharomyces cerevisiae JRY1550
brenda
Coxon, F.P.; Ebetino, F.H.; Mules, E.H.; Seabra, M.C.; McKenna, C.E.; Rogers, M.J.
Phosphonocarboxylate inhibitors of Rab geranylgeranyl transferase disrupt the prenylation and membrane localization of Rab proteins in osteoclasts in vitro and in vivo
Bone
37
349-358
2005
Mus musculus
brenda
Lackner, M.R.; Kindt, R.M.; Carroll, P.M.; Brown, K.; Cancilla, M.R.; Chen, C.; de Silva, H.; Franke, Y.; Guan, B.; Heuer, T.; Hung, T.; Keegan, K.; Lee, J.M.; Manne, V.; O'Brien, C.; Parry, D.; Perez-Villar, J.J.; Reddy, R.K.; Xiao, H.; Zhan, H.; Cockett, M.; Plowman, G.; Fitzgerald, K.; Costa, M.; Ross-Macdonald, P.
Chemical genetics identifies Rab geranylgeranyl transferase as an apoptotic target of farnesyl transferase inhibitors
Cancer Cell
7
325-336
2005
Caenorhabditis elegans, Homo sapiens
brenda
Maurer-Stroh, S.; Washietl, S.; Eisenhaber, F.
Protein prenyltransferases
Genome Biol.
4
212
2003
Homo sapiens
brenda
Wojtas, M.; Swiezewski, S.; Sarnowski, T.J.; Plochocka, D.; Chelstowska, A.; Tolmachova, T.; Swiezewska, E.
Cloning and characterization of Rab Escort Protein (REP) from Arabidopsis thaliana
Cell Biol. Int.
31
246-251
2007
Arabidopsis thaliana
brenda
Goody, R.S.; Rak, A.; Alexandrov, K.
The structural and mechanistic basis for recycling of Rab proteins between membrane compartments
Cell. Mol. Life Sci.
62
1657-1670
2005
Saccharomyces cerevisiae
brenda
Wu, Y.; Waldmann, H.; Reents, R.; Ebetino, F.H.; Goody, R.S.; Alexandrov, K.
A protein fluorescence amplifier: continuous fluorometric assay for Rab geranylgeranyltransferase
Chembiochem
7
1859-1861
2006
Rattus norvegicus
brenda
Hala, M.; Elias, M.; Zarsky, V.
A specific feature of the angiosperm Rab escort protein (REP) and evolution of the REP/GDI superfamily
J. Mol. Biol.
348
1299-1313
2005
Arabidopsis thaliana
brenda
Baron, R.A.; Seabra, M.C.
Rab geranylgeranylation occurs preferentially via the pre-formed REP-RGGT complex and is regulated by geranylgeranyl pyrophosphate
Biochem. J.
415
67-75
2008
Homo sapiens
brenda
Claessens, A.; Weyn, C.; Merregaert, J.
The cytoplasmic domain of chondrolectin interacts with the beta-subunit of Rab geranylgeranyl transferase
Cell. Mol. Biol. Lett.
13
250-259
2008
Mus musculus
brenda
Guo, Z.; Wu, Y.W.; Das, D.; Delon, C.; Cramer, J.; Yu, S.; Thuns, S.; Lupilova, N.; Waldmann, H.; Brunsveld, L.; Goody, R.S.; Alexandrov, K.; Blankenfeldt, W.
Structures of RabGGTase-substrate/product complexes provide insights into the evolution of protein prenylation
EMBO J.
27
2444-2456
2008
Rattus norvegicus
brenda
Watanabe, M.; Fiji, H.D.; Guo, L.; Chan, L.; Kinderman, S.S.; Slamon, D.J.; Kwon, O.; Tamanoi, F.
Inhibitors of protein geranylgeranyltransferase I and Rab geranylgeranyltransferase identified from a library of allenoate-derived compounds
J. Biol. Chem.
283
9571-9579
2008
Rattus norvegicus
brenda
Marma, M.S.; Xia, Z.; Stewart, C.; Coxon, F.; Dunford, J.E.; Baron, R.; Kashemirov, B.A.; Ebetino, F.H.; Triffitt, J.T.; Russell, R.G.; McKenna, C.E.
Synthesis and biological evaluation of alpha-halogenated bisphosphonate and phosphonocarboxylate analogues of risedronate
J. Med. Chem.
50
5967-5975
2007
Rattus norvegicus
brenda
Wu, Y.W.; Alexandrov, K.; Brunsveld, L.
Synthesis of a fluorescent analogue of geranylgeranyl pyrophosphate and its use in a high-throughput fluorometric assay for Rab geranylgeranyltransferase
Nat. Protoc.
2
2704-2711
2007
Rattus norvegicus
brenda
Wu, Y.W.; Goody, R.S.; Abagyan, R.; Alexandrov, K.
Structure of the disordered C terminus of Rab7 GTPase induced by binding to the Rab geranylgeranyl transferase catalytic complex reveals the mechanism of Rab prenylation
J. Biol. Chem.
284
13185-13192
2009
Homo sapiens
brenda
Baron, R.A.; Tavare, R.; Figueiredo, A.C.; B?azewska, K.M.; Kashemirov, B.A.; McKenna, C.E.; Ebetino, F.H.; Taylor, A.; Rogers, M.J.; Coxon, F.P.; Seabra, M.C.
Phosphonocarboxylates inhibit the second geranylgeranyl addition by Rab geranylgeranyl transferase
J. Biol. Chem.
284
6861-6868
2009
Homo sapiens
brenda
Tan, K.T.; Guiu-Rozas, E.; Bon, R.S.; Guo, Z.; Delon, C.; Wetzel, S.; Arndt, S.; Alexandrov, K.; Waldmann, H.; Goody, R.S.; Wu, Y.W.; Blankenfeldt, W.
Design, synthesis, and characterization of peptide-based rab geranylgeranyl transferase inhibitors
J. Med. Chem.
52
8025-8037
2009
Homo sapiens
brenda
Hala, M.; Soukupova, H.; Synek, L.; Zarsky, V.
Arabidopsis RAB geranylgeranyl transferase beta-subunit mutant is constitutively photomorphogenic, and has shoot growth and gravitropic defects
Plant J.
62
615-627
2010
Arabidopsis thaliana
brenda
Zhou, X.; Hartman, S.V.; Born, E.J.; Smits, J.P.; Holstein, S.A.; Wiemer, D.F.
Triazole-based inhibitors of geranylgeranyltransferase II
Bioorg. Med. Chem. Lett.
23
764-766
2013
Homo sapiens
brenda
Coxon, F.P.; Taylor, A.; Stewart, C.A.; Baron, R.; Seabra, M.C.; Ebetino, F.H.; Rogers, M.J.
The gunmetal mouse reveals Rab geranylgeranyl transferase to be the major molecular target of phosphonocarboxylate analogues of bisphosphonates
Bone
49
111-121
2011
Mus musculus
brenda
Arora, D.; Syed, I.; Machhadieh, B.; McKenna, C.; Kowluru, A.
Rab-geranylgeranyl transferase regulates glucose-stimulated insulin secretion from pancreatic beta cells
Islets
4
354-358
2012
Rattus norvegicus
brenda
Shi, W.; Zeng, Q.; Kunkel, B.N.; Running, M.P.
Arabidopsis Rab geranylgeranyltransferases demonstrate redundancy and broad substrate specificity in vitro
J. Biol. Chem.
291
1398-1410
2016
Arabidopsis thaliana (Q84J75), Arabidopsis thaliana (Q8VYB7), Arabidopsis thaliana (Q9FJ32), Arabidopsis thaliana (Q9LHL5), Arabidopsis thaliana
brenda
Gutkowska, M.; Wnuk, M.; Nowakowska, J.; Lichocka, M.; Stronkowski, M.M.; Swiezewska, E.
Rab geranylgeranyl transferase beta subunit is essential for male fertility and tip growth in Arabidopsis
J. Exp. Bot.
66
213-224
2015
Arabidopsis thaliana (Q84J75), Arabidopsis thaliana (Q9LHL5), Arabidopsis thaliana Col-0 (Q84J75), Arabidopsis thaliana Col-0 (Q9LHL5)
brenda
Koehnke, M.; Delon, C.; Hastie, M.L.; Nguyen, U.T.; Wu, Y.W.; Waldmann, H.; Goody, R.S.; Gorman, J.J.; Alexandrov, K.
Rab GTPase prenylation hierarchy and its potential role in choroideremia disease
PLoS ONE
8
e81758
2013
Homo sapiens
brenda
Joachimiak, L.; Marchwicka, A.; Gendaszewska-Darmach, E.; Blazewska, K.M.
Synthesis and biological evaluation of imidazole-bearing alpha-phosphonocarboxylates as inhibitors of Rab geranylgeranyl transferase (RGGT)
ChemMedChem
13
842-851
2018
Homo sapiens (P24386)
brenda
Kazmierczak, A.; Kusy, D.; Niinivehmas, S.P.; Gmach, J.; Joachimiak, L.; Pentikaeinen, O.T.; Gendaszewska-Darmach, E.; Blazewska, K.M.
Identification of the privileged position in the imidazo[1,2-a]pyridine ring of phosphonocarboxylates for development of Rab geranylgeranyl transferase (RGGT) inhibitors
J. Med. Chem.
60
8781-8800
2017
Homo sapiens (P24386)
brenda
Kuchay, S.; Wang, H.; Marzio, A.; Jain, K.; Homer, H.; Fehrenbacher, N.; Philips, M.R.; Zheng, N.; Pagano, M.
GGTase3 is a newly identified geranylgeranyltransferase targeting a ubiquitin ligase
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