VAMP4

Vesicle-associated membrane protein 4
PDB rendering based on 2nps.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2nps​
Identifiers
Symbols	VAMP4 ; VAMP-4; VAMP24
External IDs	OMIM: 606909 MGI: 1858730 HomoloGene: 37847 GeneCards: VAMP4 Gene
Gene ontology Molecular function • SNARE binding • SNAP receptor activity • protein binding Cellular component • Golgi membrane • lysosome • endosome • Golgi apparatus • trans-Golgi network • cell surface • integral component of membrane • SNARE complex Biological process • microtubule cytoskeleton organization • exocytosis • ER to Golgi vesicle-mediated transport • vesicle fusion • SNARE complex assembly • regulation of Golgi to plasma membrane protein transport • Golgi to plasma membrane protein transport • Golgi ribbon formation • toxin transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8674	53330
Ensembl	ENSG00000117533	ENSMUSG00000026696
UniProt	O75379	O70480
RefSeq (mRNA)	NM_001185127	NM_016796
RefSeq (protein)	NP_001172056	NP_058076
Location (UCSC)	Chr 1: 171.7 – 171.74 Mb	Chr 1: 162.57 – 162.6 Mb
PubMed search

Vesicle-associated membrane protein 4 is a protein that in humans is encoded by the VAMP4 gene.^[1][2]

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.^[2]

Interactions

VAMP4 has been shown to interact with AP1M1,^[3] STX6^[4] and STX16.^[4]

References

1. 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.
2. "Entrez Gene: VAMP4 vesicle-associated membrane protein 4".
3. 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.
4. 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.