Biology:GAPVD1
From HandWiki
GTPase activating protein and VPS9 domains 1, also known as GAPVD1, Gapex-5 and RME-6 is a protein which in humans is encoded by the GAPVD1 gene.[1][2]
Function
GAPVD1 is Rab GTPase guanine nucleotide exchange factor essential for activation of RAB5A during engulfment of apoptotic cells.[3] GAPVD1 is also involved in the degradation of the epidermal growth factor receptor.[4] Gapex-5 mediated activation of Rab5 has been implicated in the insulin stimulated formation of plasma membrane phosphatidylinositol-3-phosphate.[5]
Structure
Based on sequence homology, mammalian Gapex-5 has been shown to have an amino-terminal Ras GAP domain, a central polyproline (SH3 binding) region and a carboxy-terminal Rab GEF domain. The RabGEF domain has been suggested to activate Rab5[6] and Rab31.[7]
References
- ↑ "Entrez Gene: GAPVD1 GTPase activating protein and VPS9 domains 1". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=26130.
- ↑ "Rab5-activating protein 6, a novel endosomal protein with a role in endocytosis". Biochem. Biophys. Res. Commun. 340 (3): 967–75. February 2006. doi:10.1016/j.bbrc.2005.12.099. PMID 16410077.
- ↑ "Imaging of Rab5 activity identifies essential regulators for phagosome maturation". Nature 453 (7192): 241–5. May 2008. doi:10.1038/nature06857. PMID 18385674. Bibcode: 2008Natur.453..241K.
- ↑ "GAPex-5 mediates ubiquitination, trafficking, and degradation of epidermal growth factor receptor". J. Biol. Chem. 282 (29): 21278–84. July 2007. doi:10.1074/jbc.M703725200. PMID 17545148.
- ↑ "Insulin Stimulates Phosphatidylinositol 3-Phosphate Production via the Activation of Rab5". Mol. Biol. Cell 19 (7): 2718–28. July 2008. doi:10.1091/mbc.E08-01-0105. PMID 18434594.
- ↑ "Insulin-stimulated Interaction between insulin receptor substrate 1 and p85alpha and activation of protein kinase B/Akt require Rab5". J. Biol. Chem. 281 (38): 27982–90. September 2006. doi:10.1074/jbc.M602873200. PMID 16880210.
- ↑ "Gapex-5, a Rab31 Guanine Nucleotide Exchange Factor that Regulates Glut4 Trafficking in Adipocytes". Cell Metab. 5 (1): 59–72. January 2007. doi:10.1016/j.cmet.2006.12.006. PMID 17189207.
Further reading
- "GAPex-5 mediates ubiquitination, trafficking, and degradation of epidermal growth factor receptor". J. Biol. Chem. 282 (29): 21278–84. 2007. doi:10.1074/jbc.M703725200. PMID 17545148.
- "Rab5-activating protein 6, a novel endosomal protein with a role in endocytosis". Biochem. Biophys. Res. Commun. 340 (3): 967–75. 2006. doi:10.1016/j.bbrc.2005.12.099. PMID 16410077.
- "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. 2004. doi:10.1016/j.cub.2004.07.051. PMID 15324660. Bibcode: 2004CBio...14.1436J.
- "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. 2004. doi:10.1073/pnas.0404720101. PMID 15302935. Bibcode: 2004PNAS..10112130B.
- "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (2): 143–50. 2000. doi:10.1093/dnares/7.2.143. PMID 10819331.
- "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. 1997. doi:10.1101/gr.6.9.791. PMID 8889548.
- "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence". Nature 377 (6547 Suppl): 3–174. 1995. PMID 7566098. http://www.columbia.edu/itc/biology/pollack/w4065/client_edit/readings/nature377_3.pdf.
 |  |
