VAMP4

VAMP4
Identifiers
Aliases	VAMP4 , VAMP-4, VAMP24, vesicle associated membrane protein 4
External IDs	OMIM: 606909 MGI: 1858730 HomoloGene: 37847 GeneCards: VAMP4
Gene location (Human)
Chr.	Chromosome 1 (human)
End	171,742,074 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	162,426,653 bp
RNA expression pattern
	Top expressed in
	Brodmann area 23; ; substantia nigra; ; middle temporal gyrus; ; cerebellar hemisphere; ; cerebellum; ; endometrium; ; cerebellar vermis;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	SNAP receptor activity ; GO:0001948 protein binding ; SNARE binding ;
Cellular component	integral component of membrane ; cell surface ; Golgi membrane ; endosome ; Golgi apparatus ; lysosome ; membrane ; trans-Golgi network membrane ; SNARE complex ; transport vesicle ; plasma membrane ; clathrin-coated vesicle membrane ; integral component of synaptic vesicle membrane ; synaptic vesicle ;
Biological process	endoplasmic reticulum to Golgi vesicle-mediated transport ; Golgi ribbon formation ; microtubule cytoskeleton organization ; vesicle-mediated transport ; SNARE complex assembly ; Golgi to plasma membrane protein transport ; exocytosis ; membrane organization ; synaptic vesicle to endosome fusion ; regulation of synaptic vesicle endocytosis ;
	Sources:Amigo / QuickGO
Orthologs
	8674
	53330
	ENSG00000117533
	ENSMUSG00000026696
	O75379
	O70480
	NM_001185127 ; NM_003762 ; NM_201994
	NM_016796 ; NM_001347125 ; NM_001356526 ; NM_001356527
	NP_001172056 ; NP_003753
	NP_001334054 ; NP_058076 ; NP_001343455 ; NP_001343456
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 28, 2022

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]

Related Research Articles

SNARE proteins – "SNAPREceptor" – are a large protein family consisting of at least 24 members in yeasts, more than 60 members in mammalian cells, and some numbers in plants. The primary role of SNARE proteins is to mediate vesicle fusion – the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can also mediate the fusion of vesicles with membrane-bound compartments. The best studied SNAREs are those that mediate the neurotransmitter release of synaptic vesicles in neurons. These neuronal SNAREs are the targets of the neurotoxins responsible for botulism and tetanus produced by certain bacteria.

Vesicle associated membrane proteins (VAMP) are a family of SNARE proteins with similar structure, and are mostly involved in vesicle fusion.

Synaptobrevins are small integral membrane proteins of secretory vesicles with molecular weight of 18 kilodalton (kDa) that are part of the vesicle-associated membrane protein (VAMP) family.

Synaptosomal-associated protein 23 is a protein that in humans is encoded by the SNAP23 gene. Two alternative transcript variants encoding different protein isoforms have been described for this gene.

AP-1 complex subunit mu-1 is a protein that in humans is encoded by the AP1M1 gene.

Vesicle-associated membrane protein 2 (VAMP2) is a protein that in humans is encoded by the VAMP2 gene.

Synaptobrevin-like protein 1 (SYBL1), also known as vesicle-associated membrane protein 7 (VAMP7), is a protein that in humans is encoded by the VAMP7, or SYBL1, gene.

Syntaxin-7 is a protein that in humans is encoded by the STX7 gene.

Syntaxin-6 is a protein that in humans is encoded by the STX6 gene.

N-ethylmaleimide-sensitive factor Attachment Protein Alpha, also known as SNAP-α, is a SNAP protein that is involved in the intra-cellular trafficking and fusing of vesicles to target membranes in cells.

Vesicle-associated membrane protein 3 is a protein that in humans is encoded by the VAMP3 gene.

Syntaxin-5 is a protein that in humans is encoded by the STX5 gene.

Syntaxin-12 is a protein that in humans is encoded by the STX12 gene.

Vesicle-associated membrane protein 8 is a protein that in humans is encoded by the VAMP8 gene.

Syntaxin-8 is a protein that in humans is encoded by the STX8 gene. Syntaxin 8 directly interacts with HECTd3 and has similar subcellular localization. The protein has been shown to form the SNARE complex with syntaxin 7, vti1b and endobrevin. These function as the machinery for the homotypic fusion of late endosomes.

Golgi SNAP receptor complex member 1 is a protein that in humans is encoded by the GOSR1 gene.

Syntaxin-16 is a protein that in humans is encoded by the STX16 gene.

Golgi SNAP receptor complex member 2 is a protein that in humans is encoded by the GOSR2 gene.

Syntaxin-10 (STX10) is a SNARE protein that is encoded by the STX10 gene. This protein is found in most vertebrates but is noticeably absent from mice. As with other SNARE proteins, STX10 facilitates vesicle fusion and thus is important for intracellular trafficking of proteins and other cellular components. More specifically, STX10 has been implicated in endosome to Golgi trafficking of the mannose 6-phosphate receptor and glucose transporter type 4.

Vesicle transport through interaction with t-SNAREs homolog 1A is a protein that in humans is encoded by the VTI1A gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000117533 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026696 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
1 2 "Entrez Gene: VAMP4 vesicle-associated membrane protein 4".
↑ 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.
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.

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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
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. S2CID 7827573.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000117533 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026696 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9553086-5] 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.

[entrez-6] 1 2 "Entrez Gene: VAMP4 vesicle-associated membrane protein 4".

[pmid14608369-7] 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.

[pmid11839770-8] 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.

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VAMP4

Contents

Function

Interactions

Related Research Articles

References

Further reading