Vesicle-associated membrane protein 8

VAMP8
Identifiers
Aliases	VAMP8, EDB, VAMP-8, vesicle associated membrane protein 8
External IDs	OMIM: 603177; MGI: 1336882; GeneCards: VAMP8
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4WY4
Gene location (Human) Chr. Chromosome 2 (human) Band 2p11.2 Start 85,561,562 bp End 85,582,031 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6 C1|6 32.27 cM Start 72,362,206 bp End 72,367,686 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in palpebral conjunctiva monocyte mucosa of transverse colon olfactory zone of nasal mucosa granulocyte jejunal mucosa rectum nasal epithelium bronchial epithelial cell skin of abdomen Top expressed in proximal tubule right kidney yolk sac granulocyte lung bone marrow human kidney urinary bladder duodenum lip More reference expression data BioGPS More reference expression data
Gene ontology Molecular function SNAP receptor activity protein binding chloride channel inhibitor activity SNARE binding Cellular component cytoplasm integral component of membrane recycling endosome vesicle cytosol endosome early endosome membrane membrane secretory granule membrane late endosome membrane plasma membrane mucin granule lysosomal membrane SNARE complex early endosome perinuclear region of cytoplasm lysosome extracellular exosome clathrin-coated vesicle membrane phagocytic vesicle membrane azurophil granule membrane specific granule membrane recycling endosome membrane tertiary granule membrane synaptic vesicle Biological process post-Golgi vesicle-mediated transport autophagy autophagosome maturation negative regulation of secretion by cell protein transport viral entry into host cell vesicle fusion eosinophil degranulation vesicle-mediated transport mucus secretion regulation of protein localization to plasma membrane positive regulation of histamine secretion by mast cell antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent autophagosome membrane docking neutrophil degranulation membrane organization regulation of molecular function transport Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 8673 22320 Ensembl ENSG00000118640 ENSMUSG00000050732 UniProt Q9BV40 O70404 RefSeq (mRNA) NM_003761 NM_016794 RefSeq (protein) NP_003752 NP_058074 Location (UCSC) Chr 2: 85.56 – 85.58 Mb Chr 6: 72.36 – 72.37 Mb PubMed search
Wikidata
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Vesicle-associated membrane protein 8 is a protein that in humans is encoded by the VAMP8 gene.

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. It is associated with the perinuclear vesicular structures of the early endocytic compartment. It has been found that VAMP8 interacts specifically with the soluble NSF-attachment protein (alpha-SNAP), most likely through an VAMP8-containing SNARE complex. Phosphorylation of VAMP8 inside the conserved SNARE-domain can suppress vesicle fusion.

In pancreatic β-cells, VAMP8 has been shown to be part of the endosomal system. It is particularly localized to Rab11 recycling endosomes, where it plays an important role in GLP1R and GLUT2 recycling. Overexpression of VAMP8 in β-cells results in decreased insulin secretion.

Interactions

Vesicle-associated membrane protein 8 has been shown to interact with STX4, SNAP23, STX1A, STX8 and STX7.

Further reading

• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Fasshauer D, Antonin W, Margittai M, Pabst S, Jahn R (May 1999). "Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties". The Journal of Biological Chemistry. 274 (22): 15440–15446. doi:10.1074/jbc.274.22.15440. PMID 10336434.
• Kim PK, Hollerbach C, Trimble WS, Leber B, Andrews DW (December 1999). "Identification of the endoplasmic reticulum targeting signal in vesicle-associated membrane proteins". The Journal of Biological Chemistry. 274 (52): 36876–36882. doi:10.1074/jbc.274.52.36876. PMID 10601239.
• Antonin W, Holroyd C, Tikkanen R, Höning S, Jahn R (October 2000). "The R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomes". Molecular Biology of the Cell. 11 (10): 3289–3298. doi:10.1091/mbc.11.10.3289. PMC 14992. PMID 11029036.
• Antonin W, Fasshauer D, Becker S, Jahn R, Schneider TR (February 2002). "Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs". Nature Structural Biology. 9 (2): 107–111. doi:10.1038/nsb746. hdl:11858/00-001M-0000-0012-F459-F. PMID 11786915. S2CID 17724790.
• Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, et al. (April 2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–731. Bibcode:2005Natur.434..724H. doi:10.1038/nature03466. PMID 15815621.
• Brinkman JF, Ottenheim CP, de Jong LA, Zegers RH, de Smet MD, de Jong PT, et al. (August 2005). "VAMP5 and VAMP8 are most likely not involved in primary open-angle glaucoma". Molecular Vision. 11: 582–586. PMID 16110299.
• Oishi Y, Arakawa T, Tanimura A, Itakura M, Takahashi M, Tajima Y, et al. (March 2006). "Role of VAMP-2, VAMP-7, and VAMP-8 in constitutive exocytosis from HSY cells". Histochemistry and Cell Biology. 125 (3): 273–281. doi:10.1007/s00418-005-0068-y. PMID 16195891. S2CID 10541252.
• Shiffman D, Rowland CM, Louie JZ, Luke MM, Bare LA, Bolonick JI, et al. (July 2006). "Gene variants of VAMP8 and HNRPUL1 are associated with early-onset myocardial infarction". Arteriosclerosis, Thrombosis, and Vascular Biology. 26 (7): 1613–1618. doi:10.1161/01.ATV.0000226543.77214.e4. PMID 16690874.