VAMP4

VAMP4
Identifiers
AliasesVAMP4, VAMP-4, VAMP24, vesicle associated membrane protein 4
External IDsMGI: 1858730 HomoloGene: 37847 GeneCards: VAMP4
Gene location (Human)
Chr.Chromosome 1 (human)[1]
Band1q24.3Start171,700,160 bp[1]
End171,742,247 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

8674

53330

Ensembl

ENSG00000117533

ENSMUSG00000026696

UniProt

O75379

O70480

RefSeq (mRNA)

NM_001185127
NM_003762
NM_201994

NM_016796
NM_001347125
NM_001356526
NM_001356527

RefSeq (protein)

NP_001172056
NP_003753

NP_001334054
NP_058076
NP_001343455
NP_001343456

Location (UCSC)Chr 1: 171.7 – 171.74 MbChr 1: 162.57 – 162.6 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Vesicle-associated membrane protein 4 is a protein that in humans is encoded by the VAMP4 gene.[5][6]

Function

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.[6]

Interactions

VAMP4 has been shown to interact with AP1M1,[7] STX6[8] and STX16.[8]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000117533 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026696 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Advani RJ, Bae HR, Bock JB, Chao DS, Doung YC, Prekeris R, Yoo JS, Scheller RH (Apr 1998). "Seven novel mammalian SNARE proteins localize to distinct membrane compartments". The Journal of Biological Chemistry. 273 (17): 10317–24. doi:10.1074/jbc.273.17.10317. PMID 9553086.
  6. 1 2 "Entrez Gene: VAMP4 vesicle-associated membrane protein 4".
  7. ↑ Hinners I, Wendler F, Fei H, Thomas L, Thomas G, Tooze SA (Dec 2003). "AP-1 recruitment to VAMP4 is modulated by phosphorylation-dependent binding of PACS-1". EMBO Reports. 4 (12): 1182–9. doi:10.1038/sj.embor.7400018. PMC 1326413. PMID 14608369.
  8. 1 2 Mallard F, Tang BL, Galli T, Tenza D, Saint-Pol A, Yue X, Antony C, Hong W, Goud B, Johannes L (Feb 2002). "Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform". The Journal of Cell Biology. 156 (4): 653–64. doi:10.1083/jcb.200110081. PMC 2174079. PMID 11839770.

Further reading

  • Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (Apr 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
  • Steegmaier M, Klumperman J, Foletti DL, Yoo JS, Scheller RH (Jun 1999). "Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking". Molecular Biology of the Cell. 10 (6): 1957–72. doi:10.1091/mbc.10.6.1957. PMC 25394. PMID 10359608.
  • Scales SJ, Chen YA, Yoo BY, Patel SM, Doung YC, Scheller RH (May 2000). "SNAREs contribute to the specificity of membrane fusion". Neuron. 26 (2): 457–64. doi:10.1016/S0896-6273(00)81177-0. PMID 10839363.
  • Peden AA, Park GY, Scheller RH (Dec 2001). "The Di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding". The Journal of Biological Chemistry. 276 (52): 49183–7. doi:10.1074/jbc.M106646200. PMID 11598115.
  • Mallard F, Tang BL, Galli T, Tenza D, Saint-Pol A, Yue X, Antony C, Hong W, Goud B, Johannes L (Feb 2002). "Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform". The Journal of Cell Biology. 156 (4): 653–64. doi:10.1083/jcb.200110081. PMC 2174079. PMID 11839770.
  • Zeng Q, Tran TT, Tan HX, Hong W (Jun 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". The Journal of Biological Chemistry. 278 (25): 23046–54. doi:10.1074/jbc.M303214200. PMID 12682051.
  • Hinners I, Wendler F, Fei H, Thomas L, Thomas G, Tooze SA (Dec 2003). "AP-1 recruitment to VAMP4 is modulated by phosphorylation-dependent binding of PACS-1". EMBO Reports. 4 (12): 1182–9. doi:10.1038/sj.embor.7400018. PMC 1326413. PMID 14608369.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 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, Macek B, Kumar C, Mortensen P, Mann M (Nov 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.
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