Vesicle-associated membrane protein 8

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Vesicle-associated membrane protein 8 (endobrevin)
File:PBB Protein VAMP8 image.jpg
PDB rendering based on 1gl2.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols VAMP8 ; EDB; VAMP5
External IDs Template:OMIM5 Template:MGI HomoloGene: 37846
RNA expression pattern
File:PBB GE VAMP8 202546 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Vesicle-associated membrane protein 8 (endobrevin), also known as VAMP8, is a human gene.[1]

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.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: VAMP8 vesicle-associated membrane protein 8 (endobrevin)".

Further reading

  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.
  • Wong SH, Zhang T, Xu Y; et al. (1998). "Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosome". Mol. Biol. Cell. 9 (6): 1549–63. PMID 9614193.
  • Bui TD, Wong SH, Lu L, Hong W (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.
  • Fasshauer D, Antonin W, Margittai M; et al. (1999). "Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties". J. Biol. Chem. 274 (22): 15440–6. PMID 10336434.
  • Kim PK, Hollerbach C, Trimble WS; et al. (2000). "Identification of the endoplasmic reticulum targeting signal in vesicle-associated membrane proteins". J. Biol. Chem. 274 (52): 36876–82. PMID 10601239.
  • Paumet F, Le Mao J, Martin S; et al. (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. PMID 10820264.
  • Antonin W, Holroyd C, Tikkanen R; et al. (2000). "The R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomes". Mol. Biol. Cell. 11 (10): 3289–98. PMID 11029036.
  • Antonin W, Holroyd C, Fasshauer D; et al. (2001). "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. PMID 11101518.
  • Nagamatsu S, Nakamichi Y, Watanabe T; et al. (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. PMID 11112705.
  • Wade N, Bryant NJ, Connolly LM; et al. (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. PMID 11278762.
  • Antonin W, Fasshauer D, Becker S; et al. (2002). "Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs". Nat. Struct. Biol. 9 (2): 107–11. doi:10.1038/nsb746. PMID 11786915.
  • Polgár J, Chung SH, Reed GL (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. PMID 12130530.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Imai A, Nashida T, Yoshie S, Shimomura H (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. PMID 12828989.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Hillier LW, Graves TA, Fulton RS; et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
  • Brinkman JF, Ottenheim CP, de Jong LA; et al. (2006). "VAMP5 and VAMP8 are most likely not involved in primary open-angle glaucoma". Mol. Vis. 11: 582–6. PMID 16110299.
  • Oishi Y, Arakawa T, Tanimura A; et al. (2007). "Role of VAMP-2, VAMP-7, and VAMP-8 in constitutive exocytosis from HSY cells". Histochem. Cell Biol. 125 (3): 273–81. doi:10.1007/s00418-005-0068-y. PMID 16195891.
  • Shiffman D, Rowland CM, Louie JZ; et al. (2006). "Gene variants of VAMP8 and HNRPUL1 are associated with early-onset myocardial infarction". Arterioscler. Thromb. Vasc. Biol. 26 (7): 1613–8. doi:10.1161/01.ATV.0000226543.77214.e4. PMID 16690874.

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