Vesicle-associated membrane protein 8

VAMP8
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesVAMP8, EDB, VAMP-8, vesicle associated membrane protein 8
External IDsOMIM: 603177; MGI: 1336882; HomoloGene: 37846; GeneCards: VAMP8; OMA:VAMP8 - orthologs
Orthologs
SpeciesHumanMouse
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 MbChr 6: 72.36 – 72.37 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Vesicle-associated membrane protein 8 is a protein that in humans is encoded by the VAMP8 gene.[5][6][7]

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.[7] Phosphorylation of VAMP8 inside the conserved SNARE-domain can suppress vesicle fusion.[8]

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.[9]

Interactions

Vesicle-associated membrane protein 8 has been shown to interact with STX4,[10][11] SNAP23,[10][12] STX1A,[13] STX8[14] and STX7.[14][15]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000118640Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000050732Ensembl, 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.
  5. ^ Bui TD, Wong SH, Lu L, Hong W (February 1999). "Endobrevin maps to chromosome 2 in human and chromosome 6 in mouse". Genomics. 54 (3): 579–80. doi:10.1006/geno.1998.5596. PMID 9878266.
  6. ^ Wong SH, Zhang T, Xu Y, Subramaniam VN, Griffiths G, Hong W (July 1998). "Endobrevin, a Novel Synaptobrevin/VAMP-Like Protein Preferentially Associated with the Early Endosome". Mol Biol Cell. 9 (6): 1549–63. doi:10.1091/mbc.9.6.1549. PMC 25382. PMID 9614193.
  7. ^ a b "Entrez Gene: VAMP8 vesicle-associated membrane protein 8 (endobrevin)".
  8. ^ Malmersjö S, Di Palma S, Diao J, Lai Y, Pfuetzner RA, Wang AL, McMahon MA, Hayer A, Porteus M, Bodenmiller B, Brunger AT, Meyer T (July 2016). "Phosphorylation of residues inside the SNARE complex suppresses secretory vesicle fusion". EMBO Journal. 35 (16): 1721–1843. doi:10.15252/embj.201694071. PMC 5010044. PMID 27402227.
  9. ^ Liu L, Marshall M, Chadeuf E, Saras J, Barg S (2025-09-01). "VAMP8 Is an Endosomal v-SNARE That Supports GLP-1 Receptor Recycling in Pancreatic β-Cells". Diabetes. 74 (9): 1577–1588. doi:10.2337/db24-0921. ISSN 0012-1797. PMC 12365419. PMID 40608311.
  10. ^ a b Paumet F, Le Mao J, Martin S, Galli T, David B, Blank U, Roa M (June 2000). "Soluble NSF attachment protein receptors (SNAREs) in RBL-2H3 mast cells: functional role of syntaxin 4 in exocytosis and identification of a vesicle-associated membrane protein 8-containing secretory compartment". J. Immunol. 164 (11): 5850–7. doi:10.4049/jimmunol.164.11.5850. ISSN 0022-1767. PMID 10820264.
  11. ^ Polgár J, Chung Sul-Hee, Reed Guy L (August 2002). "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion". Blood. 100 (3): 1081–3. doi:10.1182/blood.V100.3.1081. ISSN 0006-4971. PMID 12130530. S2CID 36597939.
  12. ^ Imai A, Nashida Tomoko, Yoshie Sumio, Shimomura Hiromi (August 2003). "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Arch. Oral Biol. 48 (8): 597–604. doi:10.1016/S0003-9969(03)00116-X. ISSN 0003-9969. PMID 12828989.
  13. ^ Nagamatsu S, Nakamichi Y, Watanabe T, Matsushima S, Yamaguchi S, Ni J, Itagaki E, Ishida H (January 2001). "Localization of cellubrevin-related peptide, endobrevin, in the early endosome in pancreatic beta cells and its physiological function in exo-endocytosis of secretory granules". J. Cell Sci. 114 (Pt 1): 219–227. doi:10.1242/jcs.114.1.219. ISSN 0021-9533. PMID 11112705.
  14. ^ a b Antonin W, Holroyd C, Fasshauer D, Pabst S, Von Mollard G F, Jahn R (Dec 2000). "A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function". EMBO J. 19 (23): 6453–64. doi:10.1093/emboj/19.23.6453. ISSN 0261-4189. PMC 305878. PMID 11101518.
  15. ^ Wade N, Bryant N J, Connolly L M, Simpson R J, Luzio J P, Piper R C, James D E (June 2001). "Syntaxin 7 complexes with mouse Vps10p tail interactor 1b, syntaxin 6, vesicle-associated membrane protein (VAMP)8, and VAMP7 in b16 melanoma cells". J. Biol. Chem. 276 (23): 19820–7. doi:10.1074/jbc.M010838200. ISSN 0021-9258. PMID 11278762.

Further reading