Biology:VAMP3

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

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

Function

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.

Interactions

VAMP3 has been shown to interact with

• BCAP31,
• BVES,
• SNAP23,
• STX4,
• STX6.

Further reading

• "Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein". The Biochemical Journal. 320 320 ( Pt 2) (2): 429–36. December 1996. doi:10.1042/bj3200429. PMID 8973549. 
• "Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31". The Journal of Cell Biology 139 (6): 1397–410. December 1997. doi:10.1083/jcb.139.6.1397. PMID 9396746. 
• "A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells". Molecular Biology of the Cell 9 (6): 1437–48. June 1998. doi:10.1091/mbc.9.6.1437. PMID 9614185. 
• "Interaction of Munc-18-2 with syntaxin 3 controls the association of apical SNAREs in epithelial cells". Journal of Cell Science. 111 111 ( Pt 17) (17): 2681–8. September 1998. doi:10.1242/jcs.111.17.2681. PMID 9701566. 
• "Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes". The Journal of Cell Biology 143 (4): 957–71. November 1998. doi:10.1083/jcb.143.4.957. PMID 9817754. 
• "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". Journal of Immunology 164 (11): 5850–7. June 2000. doi:10.4049/jimmunol.164.11.5850. PMID 10820264. 
• "A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function". The EMBO Journal 19 (23): 6453–64. December 2000. doi:10.1093/emboj/19.23.6453. PMID 11101518. 
• "Syntaxin 7 complexes with mouse Vps10p tail interactor 1b, syntaxin 6, vesicle-associated membrane protein (VAMP)8, and VAMP7 in b16 melanoma cells". The Journal of Biological Chemistry 276 (23): 19820–7. June 2001. doi:10.1074/jbc.M010838200. PMID 11278762. 
• "Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs". Nature Structural Biology 9 (2): 107–11. February 2002. doi:10.1038/nsb746. PMID 11786915. 
• "Hyperacidification of cellubrevin endocytic compartments and defective endosomal recycling in cystic fibrosis respiratory epithelial cells". The Journal of Biological Chemistry 277 (16): 13959–65. April 2002. doi:10.1074/jbc.M105441200. PMID 11809765. 
• "Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform". The Journal of Cell Biology 156 (4): 653–64. February 2002. doi:10.1083/jcb.200110081. PMID 11839770. 
• "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. August 2002. doi:10.1182/blood.V100.3.1081. PMID 12130530. 
• "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology 21 (5): 566–9. May 2003. doi:10.1038/nbt810. PMID 12665801. 
• "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Archives of Oral Biology 48 (8): 597–604. August 2003. doi:10.1016/S0003-9969(03)00116-X. PMID 12828989. 
• "ACAP1 promotes endocytic recycling by recognizing recycling sorting signals". Developmental Cell 7 (5): 771–6. November 2004. doi:10.1016/j.devcel.2004.10.002. PMID 15525538. 
• "The variable C-terminus of cysteine string proteins modulates exocytosis and protein-protein interactions". Biochemistry 43 (51): 16212–23. December 2004. doi:10.1021/bi048612+. PMID 15610015. 
• "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. October 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.