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activated PDGFRbeta
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PI3K binding to the cytoplasmic domain of activated PDGFRbeta receptors requires phosphorylation at residues 739 and 750 and this interaction in turn activates the kinase
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adenosine
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adenosine activates PI3K and induces Akt phosphorylation leading to induction of hemeoxygenase-1, HO-1, expression in microglia. Adenosine acts as an endogenous regulator of brain inflammation via modulation of microglial reactive oxygen species production, mechanism, overview
Atg14
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PAS localization, along with that of the other components of PI3K complex I, requires Atg14
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Atg6
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in the absence of PpAtg6, PpUvrag-GFP as well as PpAtg8 fully mislocalized to the cytosol
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betagamma subunit of heterotrimeric G-proteins
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direct activation, acts synergistically with Ras
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bone morphogenetic protein-2
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activates Akt phopshorylation by PI3K. Cell treatment with BMP-2 exhibits dramatic changes in cell morphology, from a cuboid, epithelial-like shape to a spindle, fibroblastic-like appearance, consistent with epithelial-mesenchymal transition, EMT, overview
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cAMP
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PI 3-kinase is activated in response to cAMP or IGF-I, the PI 3-kinase activity bound to its p85 regulatory subunit increases by 1.7fold. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1
forskolin
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activates enzyme activity
G-protein betagamma subunits
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betagamma subunits of heterotrimeric G-protein
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IGF-I
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PI 3-kinase is activated in response to cAMP or IGF-I. cAMP-dependent PI 3-kinase activation plays an important role in the increase in cyclin D1 translation. In contrast, IGF-I-dependent PI 3-kinase activation is required for the increase in cyclin D1 mRNA levels and degradation of p27Kip1
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Insulin
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stimulates PI3K activity
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insulin-like growth factor-I
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strongly stimulates insulin receptor substrate-1-associated phosphatidylinositol 3-kinase activity about 54fold and total phosphatidylinositol 3-kinase activity abozut 6fold
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low density lipoprotein receptor-related protein 1
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LRP1, positively regulates PI3K activation. LRP1-deficient smooth muscle cells show disorganized actin in the form of membrane ruffling and enhanced cell migration, and show abnormal activation of TGFbeta signaling
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monosodium urate
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interaction of monosodium urate crystals with human neutrophils leads to the stimulation of class Ia PI-3Ks by a mechanism that is dependent on the tyrosine kinase Syk. The activation of PI-3Ks by monosodium urate crystals is a critical element regulating phospholipase D activation and degranulation of human neutrophils
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morphine
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morphine treatment enhances the level of phosphorylated, rather than unphosphorylated, PI3K and AKT, which are synchronously recruited to membrane. Levels of PTEN and p53, which are negative regulators of these signal molecules, are reduced, and as a result, the interaction between PTEN and p53 is completely interrupted
nerve growth factor
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activates the PI3-K/Akt signaling pathway
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p38 mitogen-activated protein kinase
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activates PI3K, and proteasome inactivation promotes p38 mitogen-activated protein kinase-dependent phosphatidylinositol 3-kinase activation in retinal piment epithelial cells
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phosphatidic acid
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enhances activity more markedly for PI 3-kinase II than for PI 3-kinase I
Phosphotyrosine peptides
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high-affinity activation of the enzyme requires the simultaneous binding of two phosphorylated YMXM motifs on insulin receptor substrate 1 to the two SH2 domains of the phosphatidylinositol 3'-kinase
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Ras
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acts synergistically with betagamma subunit of heterotrimeric G-proteins
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Ron kinase
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Ron plays an essential role in maintaining malignant phenotypes of colon cancer cells through regulating mutant PI3K activity
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Syk
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protein kinase Syk associates with clathrin and mediates phosphatidylinositol 3-kinase activation during human rhinovirus internalization in leukocytes
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Vps38
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the endosomal localization of Atg6 and the other components of PI3K complex II requires Vps38
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beta-catenin
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tyrosine-phopshorylated
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beta-catenin
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tyrosine-phopshorylated
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c-Src
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Dlg
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tyrosine-phopshorylated
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Dlg
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tyrosine-phopshorylated
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leptin
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1-5 nmol/L stimulates insulin receptor substrate-2 by 280-954% and its associated phosphatidylinositol-3 kinase activity 122-621%. 0.5-25 nmol/L inhibits IRS-1 pY and its associated phosphatidylinositol-3 kinase activity by 20-89%
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leptin
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increases the activity by 183% in liver at 90 ng/ml, livers and enzymes of rats with diet-induced obesity are resistant to leptin
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pioglitazone
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a thiazolidinedione, activates PI3K 2-2.5fold at 0.002-0.010 mM, activates adiponectin secretion from adipocytes in vivo
pioglitazone
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a thiazolidinedione, activates PI3K 2-2.5fold at 0.002-0.010 mM, activates adiponectin secretion from adipocytes in vivo
additional information
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insulin and IGF-I treatment increases phosphatidylinositol 3-kinase activity 4.5fold in aPY20 immunoprecipitation from whole cell lysates
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additional information
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the enzyme is activated and associated to E-cadherin complexes, the assembly is mediated by docking proteins, e.g. beta-catenin, gamma-catenin, and Dlg, and involves c-SRC. Cell-cell adhesion induces c-SRC recruitment and E-cadherin complex assembly as well as activity of PI3K, regulatory and molecular mechanism, overview. Interaction of docking proteins via the p85 subunit of PI3K
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additional information
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insulin differentially stimulates phosphatidylinositol 3-kinase activity
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additional information
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phosphoinositide-3 kinase isotype p110g is activated in vitro by both the alpha and betagamma subunits of heterotrimeric GTP-binding proteins
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additional information
phosphoinositide-3 kinase isotype p110g is activated in vitro by both the alpha and betagamma subunits of heterotrimeric GTP-binding proteins
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additional information
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b2-integrins activate the tyrosine kinases p58c-fgr and p59/61hck and causes them to associate with the p85 subunit of PtdIns 3-kinase. Thus, even if PtdIns 3-kinase is not activated by p21ras, it can maintain full enzyme activity due to the interaction with p58c-fgr or p59/61hck
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additional information
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vascular endothelial growth factor activates phosphatidylinositol 3-kinase in human umbilical vein endothelial cells. Activities of ERK, PI 3-kinase, and p70 S6 kinase are essential for vascular endothelial growth factor-induced human umbelical vein proliferation
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additional information
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p110 gamma enzyme is activated in vitro by both the alpha and beta gamma subunits of heterotrimeric guanosine triphosphate-binding proteins and does not interact with p85
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additional information
p110 gamma enzyme is activated in vitro by both the alpha and beta gamma subunits of heterotrimeric guanosine triphosphate-binding proteins and does not interact with p85
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additional information
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direct association with the activated IL-1 receptor
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additional information
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EGF stimulates phosphatidylinositol 3-kinase in human airway smooth muscle cells
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additional information
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both anti-IgM and anti-IgD stimulation results in an increase in the anti-phosphotyrosine-precipitable PI3K activity
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additional information
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microparticles, membrane vesicles released during cell activation and apoptosis, activate pathways related to NO and reactive oxygen species productions through PI3K, xanthine oxidase, and NF-kappaB pathways, overview
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additional information
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the enzyme is activated and associated to E-cadherin complexes, the assembly is mediated by docking proteins, e.g. beta-catenin, gamma-catenin, and Dlg, and involves c-SRC. Cell-cell adhesion induces c-SRC recruitment and E-cadherin complex assembly as well as activity of PI3K, regulatory and molecular mechanism, overview. Interaction of docking proteins via the p85 subunit of PI3K
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additional information
Beclin-limited model of Vps34 activation, overview. Activation of Vps34 during autophagy involves the regulated assembly of Vps34 Complex I and Complex II, driven by the release of sequestered Beclin-1 to form complexes with Vps34, Vps15 and either Atg14 or UVRAG. The availability of Beclin-1 is rate-limiting for the formation of productive Vps34 complexes
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additional information
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downstream lipid products affect the enzyme activity via effectors, enzyme activation occurs via G-protein-coupled receptors, cell adhesion, and phosphorylation by tyrosine kinase, the subunits are differently sensitive, overview
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additional information
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IL-3 and IGF-I stimulate PI 3-kinase activity
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additional information
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binding to the platelet-derived growth factor receptor transiently activates the p85a-p110a phosphoinositide 3-kinase complex in vivo
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additional information
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Fyn may be directly involved in the activation of the downstream signaling enzyme, PI3-kinase, in IL-2-stimulated T cells
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additional information
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PI3-kinase is activated by insulin and IGF-I in a rapid and transient manner in incubated soleus muscles
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additional information
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thrombopoietin induces phosphoinositol 3-kinase activation through SHP2, Gab, and insulin receptor substrate proteins in BAF3 cells and primary murine megakaryocytes
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additional information
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enzyme induction in cell culture by platelet-derived growth factor PGDF and starvation via the G-protein-coupled fMLP receptor
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additional information
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in cells loaded with protein-tyrosine phosphatase antibody, phosphatidylinositol 3'-kinase activity is increased by 38%, respectively, compared with control cells loaded with preimmune IgG
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additional information
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epidermal growth factor induces activation of phosphatidylinositol 3-kinase in rat hepatocyte primary culture
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additional information
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insulin stimulates
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additional information
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stimulation of beta1-adrenergic receptor increases the enzyme activity in cardiomyocyte via the PKA-dependent mechanism involving Gbetagamma
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