Membranes linked by trans-SNARE complexes require lipids prone to non-bilayer structure for progression to fusion
出版年份 2014 全文链接
标题
Membranes linked by trans-SNARE complexes require lipids prone to non-bilayer structure for progression to fusion
作者
关键词
-
出版物
eLife
Volume 3, Issue -, Pages -
出版商
eLife Sciences Publications, Ltd
发表日期
2014-03-05
DOI
10.7554/elife.01879
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Fusion proteins and select lipids cooperate as membrane receptors for the solubleN-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vam7p.
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- Lipid-Anchored SNAREs Lacking Transmembrane Regions Fully Support Membrane Fusion during Neurotransmitter Release
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- Membrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to small molecules and by lysis
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- (2010) William Wickner Annual Review of Cell and Developmental Biology
- Docking and Fast Fusion of Synaptobrevin Vesicles Depends on the Lipid Compositions of the Vesicle and the Acceptor SNARE Complex-Containing Target Membrane
- (2010) Marta K. Domanska et al. BIOPHYSICAL JOURNAL
- Phosphoinositides Function Asymmetrically for Membrane Fusion, Promoting Tethering and 3Q-SNARE Subcomplex Assembly
- (2010) Hao Xu et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- HOPS Initiates Vacuole Docking by Tethering Membranes before trans-SNARE Complex Assembly
- (2010) Christopher M. Hickey et al. MOLECULAR BIOLOGY OF THE CELL
- The Major Role of the Rab Ypt7p in Vacuole Fusion Is Supporting HOPS Membrane Association
- (2009) Christopher M. Hickey et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Capture and release of partially zipped trans-SNARE complexes on intact organelles
- (2009) Matthew L. Schwartz et al. JOURNAL OF CELL BIOLOGY
- Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion
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- Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components
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- The Janus-faced nature of the C2B domain is fundamental for synaptotagmin-1 function
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- Membrane fusion
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