期刊
JOURNAL OF CELL BIOLOGY
卷 158, 期 5, 页码 929-940出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200112081
关键词
SNAP-25; liposome; syntaxin; vesicle; VAMP
类别
资金
- NIDDK NIH HHS [R01 DK027044, R01 DK 27044] Funding Source: Medline
We utilize structurally targeted peptides to identify a t(C) fusion switch inherent to the coil domains of the neuronal t-SNARE that pairs with the cognate v-SNARE. The t(C) fusion switch is located in the membrane-proximal portion of the t-SNARE and controls the rate at which the helical bundle that forms the SNARE-pin can zip up to drive bilayer fusion. When the fusion switch is off (the intrinsic state of the t-SNARE), zippering of the helices from their membrane-distal ends is impeded and fusion is slow. When the t(C) fusion switch is on, fusion is much faster. The t(C) fusion switch can be thrown by a peptide that corresponds to the membrane-proximal half of the cognate v-SNARE, and binds reversibly to the cognate region of the t-SNARE. This structures the coil in the membrane-proximal domain of the t-SNARE and accelerates fusion, implying that the intrinsically unstable coil in that region is a natural impediment to the completion of zippering, and thus, fusion. Proteins that stabilize or destabilize one or the other state of the t(C) fusion switch would exert fine temporal control over the rate of fusion after SNAREs have already partly zippered up.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据