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• W2164443997 endingPage "48614" @default.
• W2164443997 startingPage "48607" @default.
• W2164443997 abstract "Rab5 and Rab4 are small monomeric GTPases localized on early endosomes and function in vesicle fusion events. These Rab proteins regulate the endocytosis and recycling or degradation of activated receptor tyrosine kinases such as the platelet-derived growth factor receptor (PDGFR). The p85α subunit of phosphatidylinositol 3′-kinase contains a BH domain with sequence homology to GTPase activating proteins (GAPs), but has not previously been shown to possess GAP activity. In this report, we demonstrate that p85α has GAP activity toward Rab5, Rab4, Cdc42, Rac1 and to a lesser extent Rab6, with little GAP activity toward Rab11. Purified recombinant Rab5 and p85α can bind directly to each other and not surprisingly, the p85α-encoded GAP activity is present in the BH domain. Because p85α stays bound to the PDGFR during receptor endocytosis, p85α will also be localized to the same early endosomal compartment as Rab5 and Rab4. Taken together, the physical co-localization and the ability of p85α to preferentially stimulate the down-regulation of Rab5 and Rab4 GTPases suggests that p85α regulates how long Rab5 and Rab4 remain in their GTP-bound active state. Cells expressing BH domain mutants of p85 show a reduced rate of PDGFR degradation as compared with wild type p85 expressing cells. These cells also show sustained activation of the mitogen-activated protein kinase and Akt pathways. Thus, the p85α protein may play a role in the down-regulation of activated receptors through its temporal control of the GTPase cycles of Rab5 and Rab4." @default.
• W2164443997 created "2016-06-24" @default.
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• W2164443997 date "2004-11-01" @default.
• W2164443997 modified "2023-09-26" @default.
• W2164443997 title "The p85α Subunit of Phosphatidylinositol 3′-Kinase Binds to and Stimulates the GTPase Activity of Rab Proteins" @default.
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• W2164443997 doi "https://doi.org/10.1074/jbc.m409769200" @default.
• W2164443997 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15377662" @default.
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