CAPS and Munc13 utilize distinct PIP2-linked mechanisms to promote vesicle exocytosis
出版年份 2013 全文链接
标题
CAPS and Munc13 utilize distinct PIP2-linked mechanisms to promote vesicle exocytosis
作者
关键词
-
出版物
MOLECULAR BIOLOGY OF THE CELL
Volume 25, Issue 4, Pages 508-521
出版商
American Society for Cell Biology (ASCB)
发表日期
2013-12-20
DOI
10.1091/mbc.e12-11-0829
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。- Coupling exo- and endocytosis: An essential role for PIP2 at the synapse
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- (2010) Neil J. Daily et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Two distinct secretory vesicle–priming steps in adrenal chromaffin cells
- (2010) Yuanyuan Liu et al. JOURNAL OF CELL BIOLOGY
- Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis
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- PIP2 Is a Necessary Cofactor for Ion Channel Function: How and Why?
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- Binding of the Munc13-1 MUN Domain to Membrane-Anchored SNARE Complexes†
- (2008) Rong Guan et al. BIOCHEMISTRY
- Phosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion
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- CAPS Facilitates Filling of the Rapidly Releasable Pool of Large Dense-Core Vesicles
- (2008) Y. Liu et al. JOURNAL OF NEUROSCIENCE
- Synaptotagmin-1 Utilizes Membrane Bending and SNARE Binding to Drive Fusion Pore Expansion
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- Synaptic vesicle fusion
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