Biology:VAMP1

Vesicle-associated membrane protein 1 (VAMP1) is a protein that in humans is encoded by the VAMP1 gene.

Function

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. VAMP1 is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Multiple alternative splice variants that encode proteins with alternative carboxy ends have been described, but the full-length nature of some variants has not been defined.

Clinical significance

Homozygous mutations in VAMP1 have been identified in a series of children affected with a form of congenital myasthenic syndrome and similar presynaptic features in these patients and the knock-out VAMP1 mouse have been demonstrated.

VAMP1 expression has been linked to higher survival rates for lung cancer patients.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.

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Nicotine Activity on Dopaminergic Neurons edit

Further reading

• "Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues". The Journal of Biological Chemistry 271 (23): 13300–3. June 1996. doi:10.1074/jbc.271.23.13300. PMID 8663154. 
• "Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2". The Biochemical Journal. 317 317 ( Pt 3) (3): 945–54. August 1996. doi:10.1042/bj3170945. PMID 8760387. 
• "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. 
• "Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMP". The Biochemical Journal. 333 333 ( Pt 2) (2): 247–51. July 1998. doi:10.1042/bj3330247. PMID 9657962. 
• "A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal". Molecular Biology of the Cell 9 (7): 1649–60. July 1998. doi:10.1091/mbc.9.7.1649. PMID 9658161. 
• "Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins". Biochemical and Biophysical Research Communications 254 (1): 21–6. January 1999. doi:10.1006/bbrc.1998.9876. PMID 9920726. 
• "VAMP-1 has a highly variable C-terminus generated by alternative splicing". Biochemical and Biophysical Research Communications 264 (3): 777–80. November 1999. doi:10.1006/bbrc.1999.1588. PMID 10544008. 
• "Munc 18a binding to syntaxin 1A and 1B isoforms defines its localization at the plasma membrane and blocks SNARE assembly in a three-hybrid system assay". Molecular and Cellular Neurosciences 20 (2): 169–80. June 2002. doi:10.1006/mcne.2002.1122. PMID 12093152. 
• "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis". Experimental Cell Research 288 (1): 35–50. August 2003. doi:10.1016/S0014-4827(03)00130-7. PMID 12878157. 
• "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.