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1,3-dihydroxy-2,2-dimethyl-5-(trifluoromethyl)-2H-benzimidazole-1,3-diium
0.1 mM, 8.0% inhibition
1,3-dihydroxy-2,2-dimethyl-5-nitro-2H-benzimidazole-1,3-diium
0.1 mM, 95.9% inhibition
1,3-dihydroxy-2,2-dimethyl-5-[(trifluoromethoxy)sulfinyl]-2H-benzimidazole-1,3-diium
0.1 mM, 64.6% inhibition
1,3-dihydroxy-5-nitrospiro[benzimidazole-1,3-diium-2,1'-cyclohexane]
0.1 mM, 99.5% inhibition
1,3-dihydroxy-5-nitrospiro[benzimidazole-1,3-diium-2,1'-cyclopentane]
0.1 mM, 96.2% inhibition
1,3-dihydroxy-5-[hydroxy(methoxy)methyl]-2,2-dimethyl-2H-benzimidazole-1,3-diium
0.1 mM, 14.6% inhibition
2-(4-carboxyphenyl)-1,3-dihydroxy-2-methyl-5-nitro-2H-benzimidazole-1,3-diium
0.1 mM, 84.1% inhibition
2-butyl-1,3-dihydroxy-2-methyl-5-nitro-2H-benzimidazole-1,3-diium
0.1 mM, 99.8% inhibition
2-ethyl-1,3-dihydroxy-2-methyl-5-nitro-2H-benzimidazole-1,3-diium
0.1 mM, 99.6% inhibition
2-ethyl-1,3-dihydroxy-5-nitro-2-propyl-2H-benzimidazole-1,3-diium
0.1 mM, 99.2% inhibition
4-bromo-1,3-dihydroxy-2,2-dimethyl-6-nitro-2H-benzimidazole-1,3-diium
0.1 mM, 100% inhibition
5-(butylamino)-1,3-dihydroxy-2,2-dimethyl-2H-benzimidazole-1,3-diium
0.1 mM, 40.9% inhibition
5-bromo-1,3-dihydroxy-2,2-dimethyl-2H-benzimidazole-1,3-diium
0.1 mM, 24.6% inhibition
5-carboxy-1,3-dihydroxy-2,2-dimethyl-2H-benzimidazole-1,3-diium
0.1 mM, 24.4% inhibition
5-ethoxy-1,3-dihydroxy-2,2-dimethyl-2H-benzimidazole-1,3-diium
0.1 mM, 21.2% inhibition
5-ethoxy-6-fluoro-1,3-dihydroxy-2,2-dimethyl-2H-benzimidazole-1,3-diium
0.1 mM, 25.2% inhibition
5-fluoro-1,3-dihydroxy-2,2-dimethyl-2H-benzimidazole-1,3-diium
0.1 mM, 35.4% inhibition
5-fluoro-1,3-dihydroxy-2,2-dimethyl-6-nitro-2H-benzimidazole-1,3-diium
0.1 mM, 60.1% inhibition
5-hexyl-1,3-dihydroxy-2,2-dimethyl-2H-benzimidazole-1,3-diium
0.1 mM, 39.3% inhibition
5-nitro-2,1,3-benzoxadiazole
0.1 mM, 43.1% inhibition
Cdc55
-
results suggest that Cdc55 acts as inhibitor downstream from shugoshin
-
Cdk1 kinase
-
phosphorylation-dependent binding of the cyclin B1 subunit of Cdk1 kinase to a Cdc6-like domain of separase inhibits separase
-
cyclin-dependent kinase 1-cyclin B1
Cdk1-cyclin B1 triggers precipitation of separase by phosphorylation but stabilizes it by inhibitory binding. Only separase that is first complexed by Cdk1-cyclin B1 can later be activated by cyclin B1 degradation
-
Pds1
Pds1 is a chaperone, inhibition of Esp1 by overexpression of undegradable Pds1 blocks mitotic exit via blockage of cohesin cleavage
-
peptide
-
acyloxymethyl ketone derivative of human SCC1 cleavage site peptide, chloromethyl ketone derivatives of the yeast Scc1 cleavage site
securin Pds1
-
an inhibitor of separase Esp1 in budding yeast. As Pds1 is degraded, Esp1 is activated, and cells transit into anaphase
securing
the motif containing H134 in securing isoform PTTG1 has a strong affinity for separase and is involved in inhibiting it, while another domain(s) in isoform is involved in activating separase and has a weaker affinity for it. Isoform PTTG2 does not interact with separase
-
sercurin
securin persistently binds and inhibits separase during much of metaphase
-
shugoshin
-
prevents separase activation independently of securin, protein phosphatase 2A coupled to regulatory subunit Cdc55 is essential for Shugoshin-mediated inhibition
-
cyclin B1
-
-
securin
-
destruction of securin occurs only upon the correct attachment of chromosomes to the spindle
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
securin
-
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
securin
inhibits separase by binding as a pseudo substrate
securin
-
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
securin
-
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
securin
-
securin homolog pimples, i.e. PIM, binds and inhibits separase
securin
-
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
securin
-
small protein that binds to and inhibits separase until all pairs of chromatids have established bipolar spindle attachments
securin
-
securin inhibits separase by blocking the access of substrates to the active site
securin
-
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. Securin is dispensable for the growth of normal human cells, in contrast to cancer cells, where depletion of PTTG1 leads to chromosome instability. The human separase-securin complex shows a whale-type distinct elongated pattern. In this complex, securin is thought to interact with the N-part of separase spanned by the ARM repeats. The N- to C-terminus intramolecular interaction in separase molecules is considered to be necessary for their catalytic activation, and this interaction is abolished by securin binding
securin
-
activity inhibited prior to the onset of the anaphase
securin
-
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
securin
-
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
securin
-
small protein that binds to and inhibits separase until all pairs of chromatids have established bipolar spindle attachments
securin
-
inhibits the proteolytic activity of separase
securin
-
securin regulates both the proteolytic and non-proteolytic activities of separase
securin
-
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. The first 156 amino acids of Esp1 seem imperative for the binding of securin Pds1, it interacts with other parts of Esp1 as well
securin
-
inhibits separase by binding as a pseudo substrate
securin
-
small protein that binds to and inhibits separase until all pairs of chromatids have established bipolar spindle attachments
securin
-
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. Interaction takes place between the N-terminus of separase and the C-terminus of securin
securin
-
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
securin
Thermochaetoides thermophila
inhibits separase by binding as a pseudo substrate
securin
-
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
additional information
-
nuclear exclusion of separase might provide the means to preclude cohesin cleavage at telophase and G1 stage of the cell cycle
-
additional information
-
separase is kept inactive in human cells by Cdk(Cdc2)-dependent phosphorylation even when securin is degraded
-
additional information
-
nuclear exclusion of separase might provide the means to preclude cohesin cleavage at telophase and G1 stage of the cell cycle
-
additional information
-
cohesin cleavage is inhibited by a PP2ACdc55-dependent mechanism
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metabolism
-
Plk1-mediated phosphorylation of Cdc6 on residue T37 promotes the interaction of Cdc6 and Cdk1, leading to the attenuation of Cdk1 activity, release of separase, and subsequent anaphase progression
evolution
-
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
evolution
-
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
evolution
-
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
evolution
-
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
evolution
-
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
evolution
-
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
evolution
-
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
evolution
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The catalytic domain of Arabidopsis separase exhibits 31 and 32% identity to the corresponding domains of human and budding yeast homologues, respectively, while the identity exceeds 50% within plant kingdom showing that the proteolytic domain of separases is the most conserved one. The sequence identity drops dramatically for the N-termini of separases. For example, the identity of the first 600 amino acid residues between Arabidopsis and Vitis vinifera separases does not exceed 39%, and it is only 30% between Arabidopsis and rice. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
evolution
-
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The catalytic domain of Arabidopsis thaliana separase exhibits 31 and 32% identity to the corresponding domains of human and budding yeast homologues, respectively. The sequence identity drops dramatically for the N-termini of separases. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
evolution
-
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The catalytic domain of Arabidopsis thaliana separase exhibits 31 and 32% identity to the corresponding domains of human and budding yeast homologues, respectively. The sequence identity drops dramatically for the N-termini of separases. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
evolution
-
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The sequence identity exceeds 50% within plant kingdom showing that the proteolytic domain of separases is the most conserved one. The sequence identity drops dramatically for the N-termini of separases. For example, the identity of the first 600 amino acid residues between Arabidopsis thaliana and Oryza sativa is only 30%. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
evolution
-
separases belong to CD clan of cysteine proteases. Unlike other members of this clan, separases are large multidomain proteins with more than 1000 amino acid residues. The sequence identity exceeds 50% within plant kingdom showing that the proteolytic domain of separases is the most conserved one. The sequence identity drops dramatically for the N-termini of separases. For example, the identity of the first 600 amino acid residues between Arabidopsis thaliana and Vitis vinifera separases does not exceed 39%. Mode of action in vivo and mechanistic differences in mitosis between organisms, overview
evolution
in-depth bioinformatical analysis of separase and generation of structural models of the two conserved domains that comprise the C-terminal region: a caspase-like domain and a putative death domain. This analysis provides insights into substrate recognition and identifies potential sites of protein-protein interactions. Both the death domain and caspase-like domain are well-conserved in separases, which suggests an evolutionary pressure to keep these two domains together, perhaps to enable separase activity and/or provide stability
evolution
in-depth bioinformatical analysis of separase and generation of structural models of the two conserved domains that comprise the C-terminal region: a caspase-like domain and a putative death domain. This analysis provides insights into substrate recognition and identifies potential sites of protein-protein interactions. Both the death domain and caspase-like domain are well-conserved in separases, which suggests an evolutionary pressure to keep these two domains together, perhaps to enable separase activity and/or provide stability
evolution
in-depth bioinformatical analysis of separase and generation of structural models of the two conserved domains that comprise the C-terminal region: a caspase-like domain and a putative death domain. This analysis provides insights into substrate recognition and identifies potential sites of protein-protein interactions. Both the death domain and caspase-like domain are well-conserved in separases, which suggests an evolutionary pressure to keep these two domains together, perhaps to enable separase activity and/or provide stability
evolution
in-depth bioinformatical analysis of separase and generation of structural models of the two conserved domains that comprise the C-terminal region: a caspase-like domain and a putative death domain. This analysis provides insights into substrate recognition and identifis potential sites of protein-protein interactions. Both the death domain and caspase-like domain are well-conserved in separases, which suggests an evolutionary pressure to keep these two domains together, perhaps to enable separase activity and/or provide stability
evolution
-
in-depth bioinformatical analysis of separase and generation of structural models of the two conserved domains that comprise the C-terminal region: a caspase-like domain and a putative death domain. This analysis provides insights into substrate recognition and identifies potential sites of protein-protein interactions. Both the death domain and caspase-like domain are well-conserved in separases, which suggests an evolutionary pressure to keep these two domains together, perhaps to enable separase activity and/or provide stability
-
malfunction
-
Arabidopsis thaliana radially swollen 4 (rsw4), a temperature-sensitive mutant, harbors a mutation in At4g22970, the separase. Loss of separase function in rsw4 at the restrictive temperature is indicated by the widespread failure of replicated chromosomes to disjoin. rsw4 has neither pronounced cell cycle arrest nor anomalous spindle formation, rsw4 roots have disorganized cortical microtubules and accumulate the mitosis-specific cyclin, cyclin B1,1
malfunction
-
loss of separase blocks centriole disengagement during mitotic exit and delays assembly of new centrioles during the following S phase
malfunction
-
loss of separase function during the early mitotic divisions causes cytokinesis failure, depletion of separase causes the accumulation of RAB-11-positive vesicles at the cleavage furrow and midbody
malfunction
-
meiotic expression of ESP RNA interference blocks the removal of cohesin during both meiosis I and II, results in alterations in nonhomologous centromere association, disrupts the radial microtubule system after telophase II, and affects the proper establishment of nuclear cytoplasmic domains, resulting in the formation of multinucleate microspores
malfunction
-
cells depleted of securin or separase display defective acidification of early endosomes and increased membrane recruitment of vacuolar ATPase complexes, mimicking the effect of the specific V-ATPase inhibitor Bafilomycin A1. Securin and separase depletion causes trans-Golgi network and endosome swelling independent of cell cycle. Endosome-mediated receptor degradation and recycling are also significantly impaired by securin and separase depletion, although not receptor internalization or Rab5 activity and autophagy
malfunction
-
cells that do not express both Cdc55 and securin prematurely separate their sister chromatids, leading to cell death
malfunction
-
cells that do not express both Cdc55 and securin prematurely separate their sister chromatids, leading to cell death
malfunction
-
cells that do not express both Cdc55 and securin prematurely separate their sister chromatids, leading to cell death. Mutant mice lacking securin and expressing a non-phosphorylatable separase die in embryonic stage. But mouse embryonic stem cells lacking both these separase regulations can still progress through mitosis in a timely fashion with correct chromosome segregation
malfunction
-
human cells with one hESP allele-encoding uncleavable protein and another allele harboring a single cleavage site grow slowly owing to cell cycle delay, in particular during G2/M transition, but not when it was expected, i.e. during anaphase
malfunction
-
in the cells lacking securin Pds1, Esp1 distribution is largely restricted to the cytoplasm
malfunction
knocking down AtESP in meiocytes using RNAi unexpectedly converts the symmetric radial microtubule systems that form after telophase II into asymmetric structures partially resembling phragmoplasts
malfunction
-
loss of either APC or separase results in a failure of the transduction of the presumed polarity signal from the centrosome cortex
malfunction
Drosophila sp. (in: flies)
-
mutations in the Drosophila Separase encoding gene Sse lead not only to endoreduplication but also telomeric fusions, suggesting a role for Sse in telomere capping
malfunction
overexpression and deregulated proteolytic activity of Separase as frequently observed in human cancers is associated with the occurrence of supernumerary centrosomes, chromosomal missegregation and aneuploidy
physiological function
-
plant separase, in addition to cleaving cohesin, regulates cyclin B1,1, with profound ramifications for morphogenesis
physiological function
-
separase acts during M phase to license centrosome duplication
physiological function
-
Separase is essential for sister chromatid separation during anaphase II. Separase-mediated proteolytic cleavage of the alpha-kleisin subunit of the cohesin complex at the metaphase-to-anaphase transition is essential for the proper segregation of chromosomes. Separase is also involved in mitotic and meiotic anaphase spindle assembly and elongation, interphase spindle pole body positioning, and epithelial cell reorganization
physiological function
-
separase is required for cytokinesis by regulating the incorporation of RAB-11-positive vesicles into the plasma membrane at the cleavage furrow and midbody
physiological function
-
separase plays a pivotal role in the separation of sister chromatids at anaphase by cleaving its substrate cohesin Rad21
physiological function
-
sister chromatid separation at anaphase is triggered by cleavage of the cohesin subunit Scc1, which is mediated by separase
physiological function
-
chromosomal segregation is mediated by cyclin-dependent kinase 1 and separase, which is regulated by cell division cycle 6, Cdc6, a mitotic substrate of polo-like kinase 1. The phosphorylation of Cdc6 by Plk1 regulates the activity of separase through the association with Cdk1
physiological function
-
function of separases in metaphase to anaphase transition, overview
physiological function
-
function of separases in metaphase to anaphase transition, overview
physiological function
-
function of separases in metaphase to anaphase transition, overview
physiological function
-
function of separases in metaphase to anaphase transition, overview. Human separase is a potential oncogene and hESP transcripts are accumulated in a large number of tumors
physiological function
-
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive
physiological function
-
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive
physiological function
-
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive
physiological function
-
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive
physiological function
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In plants, the molecular mechanisms regulating sister chromatid separation remain largely elusive. AtESP plays a role in microtubule organization or cell polarity, and an additional role for AtESP beyond cohesin cleavage
physiological function
-
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In yeasts, separase is responsible for the removal of both arm and centromeric cohesin after its phosphorylation by Cdc5 or other Plks. Esp1 action is not limited to this stage. When securin is depleted in yeast cells, the proteolytic activity of Esp1 is no longer cell cycle regulated, while Scc1 is cleaved on schedule suggesting the existence of additional regulatory elements
physiological function
-
function of separases in metaphase to anaphase transition, overview. Separase cleaves and removes the remaining centromeric cohesin. In yeasts, separase is responsible for the removal of both arm and centromeric cohesin after its phosphorylation by Cdc5 or other Plks. Separase can target both centromeric cohesin and cohesin of chromosomal arms. Cohesin is implicated in transcriptional regulation in Schizosaccharomyces pombe. When securin is depleted in yeast cells, the proteolytic activity of Esp1 is no longer cell cycle regulated, while Scc1 is cleaved on schedule suggesting the existence of additional regulatory elements
physiological function
-
function of separases in metaphase to anaphase transition, overview. The activated APCCdc20/separase pathway plays a fundamental role in the establishment of the anterior-posterior axis
physiological function
-
functional role of securin and separase in the modulation of membrane traffic and protein secretion implicating regulation of V-ATPase assembly and function. Separase activity is controlled by securin, i.e. pituitary tumor transforming gene 1, PTTG1, a member of a divergent class of anaphase inhibitors whose proteosomal degradation by the anaphase promoting complex, APC, is required to release separase and allow its activation
physiological function
-
separase Esp1 is a protease specialized in the cleavage of sister chromatid cohesion. When inhibitor securin Pds1 is degraded, Esp1 is activated, and cells transit into anaphase. Esp1, together with Clb2- and Polo-kinases, promotes Cdc14 activation through the FEAR network. Separase also leads to the activation of Cdc14 phosphatase. The phosphatase is kept inactive in the nucleolus by Net1 throughout the cell cycle until anaphase. The proteolytic function of separase causes spindle elongation by cohesin cleavage, which activates mitotic exit network, MEN, by bringing Tem1 together with its activator Lte1
physiological function
-
sister chromatid cohesion depends on the cohesin complex, a proteinaceous ring that entraps the chromatids together. At the metaphase-to-anaphase transition, separase is activated and completely dissolves the cohesion by cleaving SCC1, a subunit of the cohesin complex. As one of the key executors of anaphase, separase is regulated temporally and spatially by often redundant mechanisms. Chromosomal DNA dependent cohesin cleavage by separase is a component of a regulatory pathway that cells utilize to protect the bulk of cohesin. Degradation of securin plays a critical role in the timely activation of separase activity. But securin-independent separase regulation occur, cohesin cleavage is inhibited by a PP2ACdc55-dependent mechanism. Most of the budding yeast cohesin is cleaved in anaphase, and this cleavage is stimulated by phosphorylation of the Scc1 subunit by the Plk1 kinase
physiological function
-
sister chromatid cohesion depends on the cohesin complex, a proteinaceous ring that entraps the chromatids together. At the metaphase-to-anaphase transition, separase is activated and completely dissolves the cohesion by cleaving SCC1, a subunit of the cohesin complex. As one of the key executors of anaphase, separase is regulated temporally and spatially by often redundant mechanisms. Chromosomal DNA dependent cohesin cleavage by separase is a component of a regulatory pathway that cells utilize to protect the bulk of cohesin. Degradation of securin plays a critical role in the timely activation of separase activity. In vertebrate cells, separase is phosphorylated and inhibited before anaphase by a cyclin B/CDK1. Nuclear exclusion of separase might provide the means to preclude cohesin cleavage at telophase and G1 stage of the cell cycle
physiological function
-
sister chromatid cohesion depends on the cohesin complex, a proteinaceous ring that entraps the chromatids together. At the metaphase-to-anaphase transition, separase is activated and completely dissolves the cohesion by cleaving SCC1, a subunit of the cohesin complex. As one of the key executors of anaphase, separase is regulated temporally and spatially by often redundant mechanisms. Chromosomal DNA dependent cohesin cleavage by separase is a component of a regulatory pathway that cells utilize to protect the bulk of cohesin. Degradation of securin plays a critical role in the timely activation of separase activity. In vertebrate cells, separase is phosphorylated and inhibited before anaphase by a cyclin B/CDK1. Nuclear exclusion of separase might provide the means to preclude cohesin cleavage at telophase and G1 stage of the cell cycle
physiological function
binding between separase and cyclin B1 is required for the anaphase movement of unpaired sister chromatids. Separase promotes the reversal of Cdk1-mediated phosphorylation on chromosomes at anaphase onset
physiological function
separase acts directly on Scc1 and also indirectly, through inhibition of PP2ACdc55, to stimulate cohesin cleavage, providing a feedforward loop that may contribute to a robust and timely anaphase. PP2A activity is inhibited by separase during anaphase, triggering activation of the Cdc14 mitotic phosphatase
physiological function
separase is required at the onset of anaphase to cleave cohesin and thereby enable sister chromatid separation. The enzyme also promotes release of the Cdc14 phosphatase from the nucleolus to enable mitotic exit. The enzyme serves two roles to mediate Ty1 transposition, one to remove cohesin and the second to target Ty1-IN to chromatin
physiological function
separase is required for the separation of sister-chromatides in mitotic anaphase, triggers centriole disengagement during centrosome duplication. In cancer, separase is frequently overexpressed, pointing to a functional role as an aneuploidy promoter associated with centrosomal amplification and genomic instability
physiological function
the enzyme cleaves the Scc1/Rad21 subunit of cohesin, thereby triggering chromosome segregation
physiological function
chiasmata resolution and segregation of homologous chromosome pair. Role in DNA repair. Assembly and elongation of spindle at mitotic anaphase. Spindle formation in meiosis. Karyokinesis (division of nucleus). Spindle midzone assembly. Apoptosis promotion. Cleavage of Slk19. Cdc14 activation and release of Cdc14 from nucleolus
physiological function
-
involved in proper positioning of the centrosomes during the first asymmetric mitotic division, in the development of egg shell and in membrane trafficking
physiological function
role in DNA repair. Involved in positioning of spindle pole body
physiological function
separase cleaves the N-tail of the CENP-A related protein CPAR-1 at the meiosis I metaphase-anaphase transition
physiological function
separase cleaves the proteins that maintain the cohesion between sister chromatids
physiological function
separase cleaves the proteins that maintain the cohesion between sister chromatids
physiological function
separase cleaves the proteins that maintain the cohesion between sister chromatids
physiological function
separase cleaves the proteins that maintain the cohesion between sister chromatids
physiological function
separase is required for homolog and sister disjunction during Drosophila melanogaster male meiosis, but not for biorientation of sister centromeres
physiological function
Drosophila sp. (in: flies)
-
Separase plays an evolutionarily conserved role in telomere protection
physiological function
the enzyme is involved in cell expansion
physiological function
the enzyme is involved in establishment of cell polarity and cytokinesis, in microtubule polymerization and Kin7 activation
physiological function
the enzyme is involved in reorganization and dynamics in epithelial cells, in telomere capping and in inactivation of alternative conjunction at anaphase I onset
physiological function
the enzyme is required for centrosome duplication and separation of sister-chromatides in anaphase of mitosis
physiological function
the enzyme resolves sister chromatid cohesion during the metaphase-to-anaphase transition and plays a pivotal role in chromosomal segregation and cell division. In addition to its canonical role in the dissolution of chromosomal cohesin during metaphase to anaphase transition, separase is also implicated in centrosome cycle, membrane trafficking and DNA-damage repair
physiological function
the enzyme resolves sister chromatid cohesion during the metaphase-to-anaphase transition and plays a pivotal role in chromosomal segregation and cell division. Separase is oncogenic, and its overexpression is sufficient to induce mammary tumours in mice. Either acute or chronic overexpression of separase in mouse mammary glands leads to aneuploidy and tumorigenesis, and inhibition of separase enzymatic activity decreases the growth of human breast tumour xenografts in mice
physiological function
-
role in DNA repair. Involved in positioning of spindle pole body
-
physiological function
-
separase cleaves the proteins that maintain the cohesion between sister chromatids
-
additional information
-
cells expressing wild-type Cdc6 display lower Cdk1 activity and higher separase activity than cells expressing Cdc6 mutant T37V
additional information
-
dynamics of the mitotic exit control system in budding yeast, Queralt's model, modifications, overview. Queralt's model centres around the non-proteolytic function of separase Esp1, which triggers a positive feedback in the activation of MEN by FEAR-induced release of Cdc14
additional information
-
human separase is present in cells as a part of very large protein complex, which in addition to securin contains also Cdk and cyclin B1, both able to inhibit separase. Securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. The human separase-securin complex shows a whale-type distinct elongated pattern. In this complex, securin is thought to interact with the N-part of separase spanned by the ARM repeats. The N- to C-terminus intramolecular interaction in separase molecules is considered to be necessary for their catalytic activation, and this interaction is abolished by securin binding
additional information
-
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
additional information
-
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
additional information
-
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
additional information
-
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
additional information
-
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
additional information
-
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
additional information
-
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
additional information
-
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
additional information
-
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. Interaction takes place between the N-terminus of separase and the C-terminus of securin
additional information
-
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding. Securin is dispensable for the growth of normal human cells. The first 156 amino acids of Esp1 seem imperative for the binding of securin Pds1, it interacts with other parts of Esp1 as well. Securin is not only a guardian of separase, but is also responsible for its translocation to the nucleus in the budding yeast
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Yanagida, M.
Cell cycle mechanisms of sister chromatid separation; roles of Cut1/separin and Cut2/securin
Genes Cells
5
1-8
2000
Saccharomyces cerevisiae, Homo sapiens, Schizosaccharomyces pombe
brenda
Sullivan, M.; Lehane, C.; Uhlmann, F.
Orchestrating anaphase and mitotic exit: separase cleavage and localization of Slk19
Nat. Cell Biol.
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771-777
2001
Saccharomyces cerevisiae
brenda
Amon, A.
Together until separin do us part
Nat. Cell Biol.
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E12-14
2001
Saccharomyces cerevisiae, Homo sapiens, Schizosaccharomyces pombe
brenda
Siomos, M.F.; Badrinath, A.; Pasierbek, P.; Livingstone, D.; White, J.; Glotzer, M.; Nasmyth, K.
Separase is required for chromosome segregation during meiosis I in Caenorhabditis elegans
Curr. Biol.
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1825-1835
2001
Saccharomyces cerevisiae, Caenorhabditis elegans
brenda
Jager, H.; Herzig, A.; Lehner, C.F.; Heidmann, S.
Drosophila separase is required for sister chromatid separation and binds to PIM and THR
Genes Dev.
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2572-2584
2001
Drosophila melanogaster
brenda
Hauf, S.; Waizenegger, I.C.; Peters, J.M.
Cohesin cleavage by separase required for anaphase and cytokinesis in human cells
Science
293
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2001
Homo sapiens
brenda
Ross, K.E.; Cohen-Fix, O.
Separase: a conserved protease separating more than just sisters
Trends Cell Biol.
12
1-3
2002
Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Schizosaccharomyces pombe, Xenopus laevis
brenda
Zou, H.; Stemman, O.; Anderson, J.S.; Mann, M.; Kirschner, M.W.
Anaphase specific auto-cleavage of separase
FEBS Lett.
528
246-250
2002
Homo sapiens
brenda
Hornig, N.C.; Knowles, P.P.; McDonald, N.Q.; Uhlmann, F.
The dual mechanism of separase regulation by securin
Curr. Biol.
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973-982
2002
Saccharomyces cerevisiae
brenda
Waizenegger, I.C.; Gimenez-Abian, J.F.; Wernic, D.; Peters, J.M.
Regulation of human separase by securin binding and autocleavage
Curr. Biol.
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1368-1378
2002
Homo sapiens
brenda
Stegmeier, F.; Visintin, R.; Amon, A.
Separase, polo kinase, the kinetochore protein Slk19, and Spo12 function in a network that controls Cdc14 localization during early anaphase
Cell
108
207-220
2002
Saccharomyces cerevisiae
brenda
Buonomo, S.B.C.; Rabitsch, K.P.; Fuchs, J.; Gruber, S.; Sullivan, M.; Uhlmann, F.; Petronczki, M.; Toth, A.; Nasmyth, K.
Division of the nucleolus and its release of CDC14 during anaphase of meiosis I depends on separase, SPO12, and SLK19
Dev. Cell
4
727-739
2003
Saccharomyces cerevisiae
brenda
Sullivan, M.; Uhlmann, F.
A non-proteolytic function of separase links the onset of anaphase to mitotic exit
Nat. Cell Biol.
5
249-254
2003
Saccharomyces cerevisiae
brenda
Chestukhin, A.; Pfeffer, C.; Milligan, S.; DeCaprio, J.A.; Pellman, D.
Processing, localization, and requirement of human separase for normal anaphase progression
Proc. Natl. Acad. Sci. USA
100
4574-4579
2003
Homo sapiens
brenda
Queralt, E.; Lehane, C.; Novak, B.; Uhlmann, F.
Downregulation of PP2A(Cdc55) phosphatase by separase initiates mitotic exit in budding yeast
Cell
125
719-732
2006
Saccharomyces cerevisiae
brenda
Kudo, N.R.; Wassmann, K.; Anger, M.; Schuh, M.; Wirth, K.G.; Xu, H.; Helmhart, W.; Kudo, H.; McKay, M.; Maro, B.; Ellenberg, J.; de Boer, P.; Nasmyth, K.
Resolution of chiasmata in oocytes requires separase-mediated proteolysis
Cell
126
135-146
2006
Mus musculus (P60330), Mus musculus
brenda
Gimenez-Abian, J.F.; Diaz-Martinez, L.A.; Waizenegger, I.C.; Gimenez-Martin, G.; Clarke, D.J.
Separase is required at multiple pre-anaphase cell cycle stages in human cells
Cell Cycle
4
1576-1584
2005
Homo sapiens
brenda
Kawasaki, Y.; Nagao, K.; Nakamura, T.; Yanagida, M.
Fission yeast MAP kinase is required for the increased securin-separase interaction that rescues separase mutants under stresses
Cell Cycle
5
1831-1839
2006
Schizosaccharomyces pombe
brenda
Fan, H.Y.; Sun, Q.Y.; Zou, H.
Regulation of Separase in meiosis: Separase is activated at the metaphase I-II transition in Xenopus oocytes during meiosis
Cell Cycle
5
198-204
2006
Xenopus sp.
brenda
Terret, M.E.; Wassmann, K.; Waizenegger, I.; Maro, B.; Peters, J.M.; Verlhac, M.H.
The meiosis I-to-meiosis II transition in mouse oocytes requires separase activity
Curr. Biol.
13
1797-1802
2003
Mus musculus
brenda
Kitajima, T.S.; Miyazaki, Y.; Yamamoto, M.; Watanabe, Y.
Rec8 cleavage by separase is required for meiotic nuclear divisions in fission yeast
EMBO J.
22
5643-5653
2003
Schizosaccharomyces pombe
brenda
Nagao, K.; Yanagida, M.
Securin can have a separase cleavage site by substitution mutations in the domain required for stabilization and inhibition of separase
Genes Cells
11
247-260
2006
Schizosaccharomyces pombe
brenda
Sullivan, M.; Hornig, N.C.; Porstmann, T.; Uhlmann, F.
Studies on substrate recognition by the budding yeast separase
J. Biol. Chem.
279
1191-1196
2004
Saccharomyces cerevisiae
brenda
Wirth, K.G.; Wutz, G.; Kudo, N.R.; Desdouets, C.; Zetterberg, A.; Taghybeeglu, S.; Seznec, J.; Ducos, G.M.; Ricci, R.; Firnberg, N.; Peters, J.M.; Nasmyth, K.
Separase: a universal trigger for sister chromatid disjunction but not chromosome cycle progression
J. Cell Biol.
172
847-860
2006
Mus musculus
brenda
Pandey, R.; Heidmann, S.; Lehner, C.F.
Epithelial re-organization and dynamics of progression through mitosis in Drosophila separase complex mutants
J. Cell Sci.
118
733-742
2005
Drosophila sp. (in: flies)
brenda
Ikai, N.; Yanagida, M.
Cdc48 is required for the stability of Cut1/separase in mitotic anaphase
J. Struct. Biol.
156
50-61
2006
Schizosaccharomyces pombe
brenda
Gorr, I.H.; Boos, D.; Stemmann, O.
Mutual inhibition of separase and Cdk1 by two-step complex formation
Mol. Cell
19
135-141
2005
Xenopus sp.
brenda
Papi, M.; Berdougo, E.; Randall, C.L.; Ganguly, S.; Jallepalli, P.V.
Multiple roles for separase auto-cleavage during the G2/M transition
Nat. Cell Biol.
7
1029-1035
2005
Homo sapiens
brenda
Nagao, K.; Adachi, Y.; Yanagida, M.
Separase-mediated cleavage of cohesin at interphase is required for DNA repair
Nature
430
1044-1048
2004
Schizosaccharomyces pombe
brenda
Liu, Z.; Makaroff, C.A.
Arabidopsis separase AESP is essential for embryo development and the release of cohesin during meiosis
Plant Cell
18
1213-1225
2006
Arabidopsis thaliana (Q5IBC5), Arabidopsis thaliana
brenda
Pereira, G.; Schiebel, E.
Separase regulates INCENP-Aurora B anaphase spindle function through Cdc14
Science
302
2120-2124
2003
Saccharomyces cerevisiae
brenda
Bembenek, J.N.; Richie, C.T.; Squirrell, J.M.; Campbell, J.M.; Eliceiri, K.W.; Poteryaev, D.; Spang, A.; Golden, A.; White, J.G.
Cortical granule exocytosis in C. elegans is regulated by cell cycle components including separase
Development
134
3837-3848
2007
Caenorhabditis elegans
brenda
Shepard, J.L.; Amatruda, J.F.; Finkelstein, D.; Ziai, J.; Finley, K.R.; Stern, H.M.; Chiang, K.; Hersey, C.; Barut, B.; Freeman, J.L.; Lee, C.; Glickman, J.N.; Kutok, J.L.; Aster, J.C.; Zon, L.I.
A mutation in separase causes genome instability and increased susceptibility to epithelial cancer
Genes Dev.
21
55-59
2007
Danio rerio
brenda
Boos, D.; Kuffer, C.; Lenobel, R.; Koerner, R.; Stemmann, O.
Phosphorylation-dependent binding of cyclin B1 to a Cdc6-like domain of human separase
J. Biol. Chem.
283
816-823
2008
Homo sapiens
brenda
Nakajima, M.; Kumada, K.; Hatakeyama, K.; Noda, T.; Peters, J.M.; Hirota, T.
The complete removal of cohesin from chromosome arms depends on separase
J. Cell Sci.
120
4188-4196
2007
Homo sapiens
brenda
Pemberton, H.N.; Franklyn, J.A.; Boelaert, K.; Chan, S.Y.; Kim, D.S.; Kim, C.; Cheng, S.Y.; Kilby, M.D.; McCabe, C.J.
Separase, securin and Rad21 in neural cell growth
J. Cell. Physiol.
213
45-53
2007
Homo sapiens, Mus musculus
brenda
Gorr, I.H.; Reis, A.; Boos, D.; Wuehr, M.; Madgwick, S.; Jones, K.T.; Stemmann, O.
Essential CDK1-inhibitory role for separase during meiosis I in vertebrate oocytes
Nat. Cell Biol.
8
1035-1037
2006
Xenopus laevis
brenda
Terret, M.; Jallepalli, P.V.
Meiosis: separase strikes twice
Nat. Cell Biol.
8
910-911
2006
Saccharomyces cerevisiae, Mus musculus
brenda
Huang, X.; Andreu-Vieyra, C.V.; York, J.P.; Hatcher, R.; Lu, T.; Matzuk, M.M.; Zhang, P.
Inhibitory phosphorylation of separase is essential for genome stability and viability of murine embryonic germ cells
PLoS Biol.
6
e15
2008
Mus musculus
brenda
Adachi, Y.; Kokubu, A.; Ebe, M.; Nagao, K.; Yanagida, M.
Cut1/separase-dependent roles of multiple phosphorylation of fission yeast cohesion subunit Rad21 in post-replicative damage repair and mitosis
Cell Cycle
7
765-776
2008
Schizosaccharomyces pombe
brenda
Sak, A.; Fegers, I.; Groneberg, M.; Stuschke, M.
Effect of separase depletion on ionizing radiation-induced cell cycle checkpoints and survival in human lung cancer cell lines
Cell Prolif.
41
660-670
2008
Homo sapiens
brenda
Sun, Y.; Kucej, M.; Fan, H.Y.; Yu, H.; Sun, Q.Y.; Zou, H.
Separase is recruited to mitotic chromosomes to dissolve sister chromatid cohesion in a DNA-dependent manner
Cell
137
123-132
2009
Homo sapiens
brenda
Meyer, R.; Fofanov, V.; Panigrahi, A.; Merchant, F.; Zhang, N.; Pati, D.
Overexpression and mislocalization of the chromosomal segregation protein separase in multiple human cancers
Clin. Cancer Res.
15
2703-2710
2009
Homo sapiens
brenda
Clift, D.; Bizzari, F.; Marston, A.L.
Shugoshin prevents cohesin cleavage by PP2A(Cdc55)-dependent inhibition of separase
Genes Dev.
23
766-780
2009
Anaplasma marginale
brenda
Baskerville, C.; Segal, M.; Reed, S.I.
The protease activity of yeast separase (esp1) is required for anaphase spindle elongation independently of its role in cleavage of cohesin
Genetics
178
2361-2372
2008
Saccharomyces cerevisiae
brenda
Queralt, E.; Uhlmann, F.
Separase cooperates with Zds1 and Zds2 to activate Cdc14 phosphatase in early anaphase
J. Cell Biol.
182
873-883
2008
Saccharomyces cerevisiae
brenda
Fujita, T.; Epperly, M.W.; Zou, H.; Greenberger, J.S.; Wan, Y.
Regulation of the anaphase-promoting complex-separase cascade by transforming growth factor-beta modulates mitotic progression in bone marrow stromal cells
Mol. Biol. Cell
19
5446-5455
2008
Mus musculus
brenda
Lu, Y.; Cross, F.
Mitotic exit in the absence of separase activity
Mol. Biol. Cell
20
1576-1591
2009
Saccharomyces cerevisiae (Q03018), Saccharomyces cerevisiae
brenda
Huang, X.; Andreu-Vieyra, C.V.; Wang, M.; Cooney, A.J.; Matzuk, M.M.; Zhang, P.
Preimplantation mouse embryos depend on inhibitory phosphorylation of separase to prevent chromosome missegregation
Mol. Cell. Biol.
29
1498-1505
2009
Mus musculus
brenda
Bessat, M.; Ersfeld, K.
Functional characterization of cohesin SMC3 and separase and their roles in the segregation of large and minichromosomes in Trypanosoma brucei
Mol. Microbiol.
71
1371-1385
2009
Trypanosoma brucei
brenda
Zhang, N.; Ge, G.; Meyer, R.; Sethi, S.; Basu, D.; Pradhan, S.; Zhao, Y.J.; Li, X.N.; Cai, W.W.; El-Naggar, A.K.; Baladandayuthapani, V.; Kittrell, F.S.; Rao, P.H.; Medina, D.; Pati, D.
Overexpression of Separase induces aneuploidy and mammary tumorigenesis
Proc. Natl. Acad. Sci. USA
105
13033-13038
2008
Homo sapiens, Mus musculus
brenda
Basu, D.; Zhang, N.; Panigrahi, A.K.; Horton, T.M.; Pati, D.
Development and validation of a fluorogenic assay to measure separase enzyme activity
Anal. Biochem.
392
133-138
2009
Homo sapiens
brenda
Bembenek, J.N.; White, J.G.; Zheng, Y.
A role for separase in the regulation of RAB-11-positive vesicles at the cleavage furrow and midbody
Curr. Biol.
20
259-264
2010
Caenorhabditis elegans
brenda
Tsou, M.F.; Wang, W.J.; George, K.A.; Uryu, K.; Stearns, T.; Jallepalli, P.V.
Polo kinase and separase regulate the mitotic licensing of centriole duplication in human cells
Dev. Cell
17
344-354
2009
Homo sapiens
brenda
Katis, V.L.; Lipp, J.J.; Imre, R.; Bogdanova, A.; Okaz, E.; Habermann, B.; Mechtler, K.; Nasmyth, K.; Zachariae, W.
Rec8 phosphorylation by casein kinase 1 and Cdc7-Dbf4 kinase regulates cohesin cleavage by separase during meiosis
Dev. Cell
18
397-409
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae SK1
brenda
Wu, S.; Scheible, W.R.; Schindelasch, D.; Van Den Daele, H.; De Veylder, L.; Baskin, T.I.
A conditional mutation in Arabidopsis thaliana separase induces chromosome non-disjunction, aberrant morphogenesis and cyclin B1,1 stability
Development
137
953-961
2010
Arabidopsis thaliana
brenda
Nakamura, A.; Arai, H.; Fujita, N.
Centrosomal Aki1 and cohesin function in separase-regulated centriole disengagement
J. Cell Biol.
187
607-614
2009
Homo sapiens
brenda
Kudo, N.R.; Anger, M.; Peters, A.H.; Stemmann, O.; Theussl, H.C.; Helmhart, W.; Kudo, H.; Heyting, C.; Nasmyth, K.
Role of cleavage by separase of the Rec8 kleisin subunit of cohesin during mammalian meiosis I
J. Cell Sci.
122
2686-2698
2009
Homo sapiens
brenda
Ishiguro, T.; Tanaka, K.; Sakuno, T.; Watanabe, Y.
Shugoshin-PP2A counteracts casein-kinase-1-dependent cleavage of Rec8 by separase
Nat. Cell Biol.
12
500-506
2010
Homo sapiens
brenda
Yang, X.; Boateng, K.A.; Strittmatter, L.; Burgess, R.; Makaroff, C.A.
Arabidopsis separase functions beyond the removal of sister chromatid cohesion during meiosis
Plant Physiol.
151
323-333
2009
Arabidopsis thaliana
brenda
Vinod, P.K.; Freire, P.; Rattani, A.; Ciliberto, A.; Uhlmann, F.; Novak, B.
Computational modelling of mitotic exit in budding yeast: the role of separase and Cdc14 endocycles
J. R. Soc. Interface
8
1128-1141
2011
Saccharomyces cerevisiae
brenda
Kucej, M.; Zou, H.
DNA-dependent cohesin cleavage by separase
Nucleus
1
4-7
2011
Saccharomyces cerevisiae, Homo sapiens, Mus musculus
brenda
Moschou, P.N.; Bozhkov, P.V.
Separases: biochemistry and function
Physiol. Plant.
145
67-76
2012
Saccharomyces cerevisiae, Caenorhabditis elegans, Ricinus communis, Chlamydomonas reinhardtii, Drosophila melanogaster, Homo sapiens, Oryza sativa, Schizosaccharomyces pombe, Sorghum bicolor, Vitis vinifera, Cryptosporidium muris, Arabidopsis thaliana (Q5IBC5)
brenda
Yim, H.; Erikson, R.L.
Cell division cycle 6, a mitotic substrate of polo-like kinase 1, regulates chromosomal segregation mediated by cyclin-dependent kinase 1 and separase
Proc. Natl. Acad. Sci. USA
107
19742-19747
2010
Homo sapiens
brenda
Bacac, M.; Fusco, C.; Planche, A.; Santodomingo, J.; Demaurex, N.; Leemann-Zakaryan, R.; Provero, P.; Stamenkovic, I.
Securin and separase modulate membrane traffic by affecting endosomal acidification
Traffic
12
615-626
2011
Homo sapiens
brenda
Matsuo, K.; Ohsumi, K.; Iwabuchi, M.; Kawamata, T.; Ono, Y.; Takahashi, M.
Kendrin is a novel substrate for separase involved in the licensing of centriole duplication
Curr. Biol.
22
915-921
2012
Homo sapiens (Q14674)
brenda
Shindo, N.; Kumada, K.; Hirota, T.
Separase sensor reveals dual roles for separase coordinating cohesin cleavage and cdk1 inhibition
Dev. Cell
23
112-123
2012
Mus musculus (P60330)
brenda
Yaakov, G.; Thorn, K.; Morgan, D.O.
Separase biosensor reveals that cohesin cleavage timing depends on phosphatase PP2A(Cdc55) regulation
Dev. Cell
23
124-136
2012
Saccharomyces cerevisiae (Q03018), Saccharomyces cerevisiae
brenda
Hellmuth, S.; Poehlmann, C.; Brown, A.; Boettger, F.; Sprinzl, M.; Stemmann, O.
Positive and negative regulation of vertebrate separase by cdk1-cyclin b1 may explain why securin is dispensable
J. Biol. Chem.
290
8002-8010
2015
Homo sapiens (Q14674)
brenda
Han, X.; Poon, R.Y.
Critical differences between isoforms of securin reveal mechanisms of separase regulation
Mol. Cell. Biol.
33
3400-3415
2013
Saccharomyces cerevisiae (Q03018)
brenda
Agircan, F.G.; Schiebel, E.
Sensors at centrosomes reveal determinants of local separase activity
PLoS Genet.
10
e1004672
2014
Homo sapiens (Q14674)
brenda
Ho, K.L.; Ma, L.; Cheung, S.; Manhas, S.; Fang, N.; Wang, K.; Young, B.; Loewen, C.; Mayor, T.; Measday, V.
A role for the budding yeast separase, Esp1, in Ty1 element retrotransposition
PLoS Genet.
11
e1005109
2015
Saccharomyces cerevisiae (Q03018), Saccharomyces cerevisiae
brenda
Haass, W.; Stehle, M.; Nittka, S.; Giehl, M.; Schrotz-King, P.; Fabarius, A.; Hofmann, W.K.; Seifarth, W.
The proteolytic activity of separase in BCR-ABL-positive cells is increased by imatinib
PLoS ONE
7
e42863
2012
Homo sapiens (Q14674), Homo sapiens
brenda
Zhang, N.; Pati, D.
Biology and insights into the role of cohesin protease separase in human malignancies
Biol. Rev. Camb. Philos. Soc.
92
2070-2083
2017
Mus musculus (P60330), Mus musculus, Homo sapiens (Q14674), Homo sapiens
brenda
Do, H.T.; Zhang, N.; Pati, D.; Gilbertson, S.R.
Synthesis and activity of benzimidazole-1,3-dioxide inhibitors of separase
Bioorg. Med. Chem. Lett.
26
4446-4450
2016
Homo sapiens (Q14674), Homo sapiens
brenda
Luo, S.; Tong, L.
Structural biology of the separase-securin complex with crucial roles in chromosome segregation
Curr. Opin. Struct. Biol.
49
114-122
2018
Saccharomyces cerevisiae, Thermochaetoides thermophila (G0SHM3), Caenorhabditis elegans (G5ED39), Caenorhabditis elegans, Thermochaetoides thermophila DSM 1495 (G0SHM3)
brenda
Kumar, R.
Separase Function beyond cohesion cleavage and an emerging oncogene
J. Cell. Biochem.
118
1283-1299
2017
Caenorhabditis elegans, Arabidopsis thaliana (A0A1P8B3N4), Schizosaccharomyces pombe (P18296), Saccharomyces cerevisiae (Q03018), Drosophila melanogaster (Q9VRN6), Picea abies (R4XPW1), Schizosaccharomyces pombe ATCC 24843 (P18296)
brenda
Cipressa, F.; Morciano, P.; Bosso, G.; Mannini, L.; Galati, A.; Raffa, G.D.; Cacchione, S.; Musio, A.; Cenci, G.
A role for Separase in telomere protection
Nat. Commun.
7
10405
2016
Drosophila sp. (in: flies)
brenda
Lin, Z.; Luo, X.; Yu, H.
Structural basis of cohesin cleavage by separase
Nature
532
131-134
2016
Thermochaetoides thermophila (G0SHM3), Thermochaetoides thermophila DSM 1495 (G0SHM3)
brenda
Winter, A.; Schmid, R.; Bayliss, R.
Structural insights into separase architecture and substrate recognition through computational modelling of caspase-like and death domains
PLoS Comput. Biol.
11
e1004548
2015
Caenorhabditis elegans (G5ED39), Caenorhabditis elegans, Saccharomyces cerevisiae (Q03018), Homo sapiens (Q14674), Arabidopsis thaliana (Q5IBC5), Saccharomyces cerevisiae ATCC 204508 (Q03018)
brenda
Blattner, A.C.; Chaurasia, S.; McKee, B.D.; Lehner, C.F.
Separase is required for homolog and sister disjunction during Drosophila melanogaster male meiosis, but not for biorientation of sister centromeres
PLoS Genet.
12
e1005996
2016
Drosophila melanogaster (Q9VRN6), Drosophila melanogaster
brenda
Monen, J.; Hattersley, N.; Muroyama, A.; Stevens, D.; Oegema, K.; Desai, A.
Separase cleaves the N-tail of the CENP-A related protein CPAR-1 at the meiosis I metaphase-anaphase transition in C. elegans
PLoS ONE
10
e0125382
2015
Caenorhabditis elegans (G5ED39), Caenorhabditis elegans
brenda
Haass, W.; Kleiner, H.; Mueller, M.C.; Hofmann, W.K.; Fabarius, A.; Seifarth, W.
Measurement of separase proteolytic activity in single living cells by a fluorogenic flow cytometry assay
PLoS ONE
10
e0133769
2015
Homo sapiens (Q14674), Homo sapiens
brenda