期刊
TRENDS IN NEUROSCIENCES
卷 32, 期 5, 页码 275-282出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tins.2009.01.004
关键词
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资金
- Israel Science Foundation [1211/07]
- Adams Super Center for Brain Studies
- National Institutes of Health [1101 NS053978]
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R01NS053978] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE ON AGING [ZIAAG000317] Funding Source: NIH RePORTER
Priming is the process by which vesicles become available for fusion at nerve terminals and is modulated by numerous proteins and second messengers. One of the prominent members of this diverse family is tomosyn. Tomosyn has been identified as a syntaxin-binding protein; it inhibits vesicle priming, but its mode of action is not fully understood. The inhibitory activity of tomosyn depends on its N-terminal WD40-repeat domain and is regulated by the binding of its SNARE motif to syntaxin. Here, we describe new physiological information on the function of tomosyn and address possible interpretations of these results in the framework of the recently described crystal structure of the yeast tomosyn homolog Sro7. We also present possible molecular scenarios for vesicle priming and the involvement of tomosyn in these processes.
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