VAMP3

From Wikipedia, the free encyclopedia


Vesicle-associated membrane protein 3 (cellubrevin)
PDB rendering based on 1kil.
Available structures: 1kil, 1n7s
Identifiers
Symbol(s) VAMP3; CEB
External IDs OMIM: 603657 MGI1321389 HomoloGene3511
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 9341 22319
Ensembl ENSG00000049245 ENSMUSG00000028955
Uniprot Q15836 P63024
Refseq NM_004781 (mRNA)
NP_004772 (protein)
NM_009498 (mRNA)
NP_033524 (protein)
Location Chr 1: 7.75 - 7.76 Mb Chr 4: 149.89 - 149.9 Mb
Pubmed search [1] [2]

Vesicle-associated membrane protein 3 (cellubrevin), also known as VAMP3, is a human gene.[1]

Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. This gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Because of its high homology to other known VAMPs, its broad tissue distribution, and its subcellular localization, the protein encoded by this gene was shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.[1]

[edit] References

[edit] Further reading

  • Timmers KI, Clark AE, Omatsu-Kanbe M, et al. (1997). "Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein.". Biochem. J. 320 ( Pt 2): 429–36. PMID 8973549. 
  • Annaert WG, Becker B, Kistner U, et al. (1998). "Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31.". J. Cell Biol. 139 (6): 1397–410. PMID 9396746. 
  • Galli T, Zahraoui A, Vaidyanathan VV, et al. (1998). "A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells.". Mol. Biol. Cell 9 (6): 1437–48. PMID 9614185. 
  • Riento K, Galli T, Jansson S, et al. (1999). "Interaction of Munc-18-2 with syntaxin 3 controls the association of apical SNAREs in epithelial cells.". J. Cell. Sci. 111 ( Pt 17): 2681–8. PMID 9701566. 
  • Prekeris R, Klumperman J, Chen YA, Scheller RH (1998). "Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes.". J. Cell Biol. 143 (4): 957–71. PMID 9817754. 
  • Bernstein AM, Whiteheart SW (1999). "Identification of a cellubrevin/vesicle associated membrane protein 3 homologue in human platelets.". Blood 93 (2): 571–9. PMID 9885218. 
  • 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, 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. 
  • 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. 
  • Poschet JF, Skidmore J, Boucher JC, et al. (2002). "Hyperacidification of cellubrevin endocytic compartments and defective endosomal recycling in cystic fibrosis respiratory epithelial cells.". J. Biol. Chem. 277 (16): 13959–65. doi:10.1074/jbc.M105441200. PMID 11809765. 
  • Mallard F, Tang BL, Galli T, et al. (2002). "Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform.". J. Cell Biol. 156 (4): 653–64. doi:10.1083/jcb.200110081. PMID 11839770. 
  • 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. 
  • Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. 
  • 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. 
  • Dai J, Li J, Bos E, et al. (2004). "ACAP1 promotes endocytic recycling by recognizing recycling sorting signals.". Dev. Cell 7 (5): 771–6. doi:10.1016/j.devcel.2004.10.002. PMID 15525538. 
  • Boal F, Zhang H, Tessier C, et al. (2005). "The variable C-terminus of cysteine string proteins modulates exocytosis and protein-protein interactions.". Biochemistry 43 (51): 16212–23. doi:10.1021/bi048612. PMID 15610015. 
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.