α/β/γ/ SNAP
Peripheral membrane proteins required for membrane traffic
References SySy α/β/γ/ SNAP antibodies
Burgalossi A, Jung S, Meyer G, Jockusch WJ, Jahn O, Taschenberger H, O'Connor VM, Nishiki T, Takahashi M, Brose N & Rhee JS (2010). SNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle priming. Neuron 68: 473-87. γSNAP; WBGreaves J & Chamberlain LH. (2006). Dual role of the cysteine-string domain in membrane binding and palmitoylation-dependent sorting of the molecular chaperone cysteine-string protein. Molecular Biology of the Cell 17: 4748-59. MABs; WB
Tian JH, Wu ZX, Unzicker M, Lu L, Cai Q, Li C, Schirra C, Matti U, Stevens D, Deng C, Rettig J & Sheng ZH (2005). The role of Snapin in neurosecretion: snapin knock-out mice exhibit impaired calcium-dependent exocytosis of large dense-core vesicles in chromaffin cells. Journal of Neuroscience 25: 10546-55. MABs; WB
Tomes CN, De Blas GA, Michaut MA, Farré EV, Cherhitin O, Visconti PE & Mayorga LS (2005). alpha-SNAP and NSF are required in a priming step during the human sperm acrosome reaction. Molecular Human Reproduction 11: 43-51. MABs; WB
Dalal S, Rosser MFN, Cyr DM & Hanson PI (2004). Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway. Molecular Biology of the Cell 15: 637-48.
Chamberlain LH, Burgoyne RD & Gould GW (2001). SNARE proteins are highly enriched in lipid rafts in PC12 cells: Implications for the spatial control of exocytosis. Proceedings of the National Academy of Sciences USA 99: 5619-24. MABs; WB
Graham ME & Burgoyne RD (2000). Comparison of cysteine string protein (Csp) and mutant alpha-SNAP overexpression reveals a role for csp in late steps of membrane fusion in dense-core granule exocytosis in adrenal chromaffin cells. Journal of Neuroscience 20: 1281-9.
von Kriegstein K, Schmitz F, Link E & Sudhof T (1999). Distribution of synaptic vesicle proteins in the mammalian retina identifies obligatory and facultative components of ribbon synapses. European Journal of Neuroscience 11: 1335-48.
Steel GJ, Laude AJ, Boojawan A, Harvey DJ & Morgan A (1999). Biochemical analysis of the Saccharomyces cereVisiae SEC18 gene product: implications for the molecular mechanism of membrane fusion. Biochemistry 38: 7764-72.
Hanson PI, Otto H, Barton N & Jahn R (1995). The N-ethylmaleimide sensitive fusion protein and α-SNAP induce a conformational change in syntaxin. Journal of Biological Chemistry 270: 16955-61. Description of clones 77.1 and 77.2
General references α/β/γ/ SNAP
Tani K, Shibata M, Kawase K, Kawashima H, Hatsuzawa K, Nagahama M & Tagaya M (2003). Mapping of functional domains of gamma-SNAP. Journal of Biological Chemistry 278: 13531-8.Lin RC & Scheller RH (2000). Mechanisms of synaptic vesicle exocytosis. Annual Review of Cell & Developmental Biology 16: 19-49. Review
Jahn R & Südhof TC (1999). Membrane fusion ans exocytosis. Annual Review of Biochemistry 68: 863-911. Review
Peter F, Wong SH, Subramaniam VN, Tang BL & Hong W (1998). Alpha-SNAP but not gamma-SNAP is required for ER-Golgi transport after vesicle budding and the Rab1-requiring step but before the EGTA-sensitive step. Journal of Cell Science 111(Pt 17): 2625-33.
Südhof TC (1995). The synaptic vesicle cycle: a cascade of protein- protein interactions. Nature 375: 645-53. Review
Rothman JE (1994). Mechanisms of intracellular protein transport. Nature 372: 55-63. Review
