VAMP4

From Wikipedia, the free encyclopedia


Vesicle-associated membrane protein 4
PDB rendering based on 2nps.
Available structures: 2nps
Identifiers
Symbol(s) VAMP4; VAMP24
External IDs OMIM: 606909 MGI1858730 HomoloGene37847
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 8674 53330
Ensembl ENSG00000117533 ENSMUSG00000026696
Uniprot O75379 Q9D095
Refseq NM_003762 (mRNA)
NP_003753 (protein)
NM_016796 (mRNA)
NP_058076 (protein)
Location Chr 1: 169.94 - 169.98 Mb Chr 1: 164.41 - 164.44 Mb
Pubmed search [1] [2]

Vesicle-associated membrane protein 4, also known as VAMP4, is a human gene.[1]

Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. The protein encoded by this gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. This protein may play a role in trans-Golgi network-to-endosome transport.[1]

[edit] References

[edit] Further reading

  • Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107-13. doi:10.1006/abio.1996.0138. PMID 8619474. 
  • Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353-8. PMID 9110174. 
  • Advani RJ, Bae HR, Bock JB, et al. (1998). "Seven novel mammalian SNARE proteins localize to distinct membrane compartments.". J. Biol. Chem. 273 (17): 10317-24. PMID 9553086. 
  • Steegmaier M, Klumperman J, Foletti DL, et al. (1999). "Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking.". Mol. Biol. Cell 10 (6): 1957-72. PMID 10359608. 
  • Scales SJ, Chen YA, Yoo BY, et al. (2000). "SNAREs contribute to the specificity of membrane fusion.". Neuron 26 (2): 457-64. PMID 10839363. 
  • Peden AA, Park GY, Scheller RH (2002). "The Di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding.". J. Biol. Chem. 276 (52): 49183-7. doi:10.1074/jbc.M106646200. PMID 11598115. 
  • Mallard F, Tang BL, Galli T, et al. (2002). "Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform.". J. Cell Biol. 156 (4): 653-64. doi:10.1083/jcb.200110081. PMID 11839770. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Zeng Q, Tran TT, Tan HX, Hong W (2003). "The cytoplasmic domain of Vamp4 and Vamp5 is responsible for their correct subcellular targeting: the N-terminal extenSion of VAMP4 contains a dominant autonomous targeting signal for the trans-Golgi network.". J. Biol. Chem. 278 (25): 23046-54. doi:10.1074/jbc.M303214200. PMID 12682051. 
  • Hinners I, Wendler F, Fei H, et al. (2004). "AP-1 recruitment to VAMP4 is modulated by phosphorylation-dependent binding of PACS-1.". EMBO Rep. 4 (12): 1182-9. doi:10.1038/sj.embor.7400018. PMID 14608369. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173-8. doi:10.1038/nature04209. PMID 16189514. 
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635-48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.