Identification of SNAP-47, a novel Qbc-SNARE with ubiquitous expression.

作者: Matthew Holt , Frédérique Varoqueaux , Katrin Wiederhold , Shigeo Takamori , Henning Urlaub

DOI: 10.1074/JBC.M513838200

关键词:

摘要: The SNARE proteins are essential components of the intracellular fusion machinery. It is thought that they form a tight four-helix complex between membranes, in effect initiating fusion. Most SNAREs contain single coiled-coil region, referred to as motif, directly adjacent transmembrane domain. neuronal SNAP-25 defines subfamily with two helices connected by longer linker, comprising also SNAP-23 and SNAP-29. We now report initial characterization novel vertebrate homologue termed SNAP-47. Northern blot immunoblot analysis revealed ubiquitous tissue distribution, particularly high levels nervous tissue. In neurons, SNAP-47 shows widespread distribution on membranes enriched synaptic vesicle fractions. vitro, substituted for formation syntaxin 1a synaptobrevin 2, it proteoliposome However, neither assembly nor was efficient SNAP-25.

参考文章(42)
Darshan K. Koticha, Giulia Baldini, Ellen E. McCarthy, Plasma membrane targeting of SNAP-25 increases its local concentration and is necessary for SNARE complex formation and regulated exocytosis. Journal of Cell Science. ,vol. 115, pp. 3341- 3351 ,(2002) , 10.1242/JCS.115.16.3341
Jung-Hwa Tao-Cheng, Jing Du, Chris J. McBain, Snap-25 is polarized to axons and abundant along the axolemma: an immunogold study of intact neurons. Journal of Neurocytology. ,vol. 29, pp. 67- 77 ,(2000) , 10.1023/A:1007168231323
Yu A. Chen, Richard H. Scheller, SNARE-mediated membrane fusion Nature Reviews Molecular Cell Biology. ,vol. 2, pp. 98- 106 ,(2001) , 10.1038/35052017
R. Bryan Sutton, Dirk Fasshauer, Reinhard Jahn, Axel T. Brunger, Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution Nature. ,vol. 395, pp. 347- 353 ,(1998) , 10.1038/26412
C Chen, H Okayama, High-efficiency transformation of mammalian cells by plasmid DNA. Molecular and Cellular Biology. ,vol. 7, pp. 2745- 2752 ,(1987) , 10.1128/MCB.7.8.2745
Juan S Bonifacino, Benjamin S Glick, The Mechanisms of Vesicle Budding and Fusion Cell. ,vol. 116, pp. 153- 166 ,(2004) , 10.1016/S0092-8674(03)01079-1
Philip WASHBOURNE, Victor CANSINO, James R. MATHEWS, Margaret GRAHAM, Robert D. BURGOYNE, Michael C. WILSON, Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting. Biochemical Journal. ,vol. 357, pp. 625- 634 ,(2001) , 10.1042/0264-6021:3570625
Bin Yang, Lino Gonzalez, Rytis Prekeris, Martin Steegmaier, Raj J. Advani, Richard H. Scheller, SNARE Interactions Are Not Selective: IMPLICATIONS FOR MEMBRANE FUSION SPECIFICITY Journal of Biological Chemistry. ,vol. 274, pp. 5649- 5653 ,(1999) , 10.1074/JBC.274.9.5649
C. G. Schuette, K. Hatsuzawa, M. Margittai, A. Stein, D. Riedel, P. Kuster, M. Konig, C. Seidel, R. Jahn, Determinants of liposome fusion mediated by synaptic SNARE proteins. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 101, pp. 2858- 2863 ,(2004) , 10.1073/PNAS.0400044101
Veerasamy Ravichandran, Ashish Chawla, Paul A. Roche, Identification of a Novel Syntaxin- and Synaptobrevin/VAMP-binding Protein, SNAP-23, Expressed in Non-neuronal Tissues Journal of Biological Chemistry. ,vol. 271, pp. 13300- 13303 ,(1996) , 10.1074/JBC.271.23.13300