GAPVD1

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GAPVD1
Identifiers
Aliases GAPVD1, GAPEX5, GAPex-5, RAP6, GTPase activating protein and VPS9 domains 1
External IDs MGI: 1913941 HomoloGene: 32637 GeneCards: GAPVD1
Gene location (Human)
Chromosome 9 (human)
Chr. Chromosome 9 (human)[1]
Chromosome 9 (human)
Genomic location for GAPVD1
Genomic location for GAPVD1
Band 9q33.3 Start 125,261,794 bp[1]
End 125,367,207 bp[1]
RNA expression pattern
PBB GE GAPVD1 212804 s at fs.png

PBB GE GAPVD1 214869 x at fs.png

PBB GE GAPVD1 212802 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_025709
NM_001356441

RefSeq (protein)

NP_079985
NP_001343370

Location (UCSC) Chr 9: 125.26 – 125.37 Mb Chr 9: 34.67 – 34.76 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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.[5][6]

Function[edit]

GAPVD1 is Rab GTPase guanine nucleotide exchange factor essential for activation of RAB5A during engulfment of apoptotic cells.[7] GAPVD1 is also involved in the degradation of the epidermal growth factor receptor.[8] Gapex-5 mediated activation of Rab5 has been implicated in the insulin stimulated formation of plasma membrane phosphatidylinositol-3-phosphate.[9]

Structure[edit]

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[10] and Rab31.[11]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000165219 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026867 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ "Entrez Gene: GAPVD1 GTPase activating protein and VPS9 domains 1". 
  6. ^ Hunker CM, Galvis A, Kruk I, Giambini H, Veisaga ML, Barbieri MA (February 2006). "Rab5-activating protein 6, a novel endosomal protein with a role in endocytosis". Biochem. Biophys. Res. Commun. 340 (3): 967–75. doi:10.1016/j.bbrc.2005.12.099. PMID 16410077. 
  7. ^ Kitano M, Nakaya M, Nakamura T, Nagata S, Matsuda M (May 2008). "Imaging of Rab5 activity identifies essential regulators for phagosome maturation". Nature. 453 (7192): 241–5. doi:10.1038/nature06857. PMID 18385674. 
  8. ^ Su X, Kong C, Stahl PD (July 2007). "GAPex-5 mediates ubiquitination, trafficking, and degradation of epidermal growth factor receptor". J. Biol. Chem. 282 (29): 21278–84. doi:10.1074/jbc.M703725200. PMID 17545148. 
  9. ^ Lodhi IJ, Bridges D, Chiang SH, Zhang Y, Cheng A, Geletka LM, Weisman LS, Saltiel AR (July 2008). "Insulin Stimulates Phosphatidylinositol 3-Phosphate Production via the Activation of Rab5". Mol. Biol. Cell. 19 (7): 2718–28. doi:10.1091/mbc.E08-01-0105. PMC 2441665Freely accessible. PMID 18434594. 
  10. ^ Su X, Lodhi IJ, Saltiel AR, Stahl PD (September 2006). "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. doi:10.1074/jbc.M602873200. PMID 16880210. 
  11. ^ Lodhi IJ, Chiang SH, Chang L, Vollenweider D, Watson RT, Inoue M, Pessin JE, Saltiel AR (January 2007). "Gapex-5, a Rab31 Guanine Nucleotide Exchange Factor that Regulates Glut4 Trafficking in Adipocytes". Cell Metab. 5 (1): 59–72. doi:10.1016/j.cmet.2006.12.006. PMC 1779820Freely accessible. PMID 17189207. 

Further reading[edit]