期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
卷 1851, 期 6, 页码 785-793出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbalip.2014.09.017
关键词
Phosphatidylinositol(4,5)bisphosphate; Vesicle exocytosis; CAPS/CADPS; Munc13; Synaptotagmin; SNARE protein
资金
- NIH [DK025861, DK040428]
PI(4,5)P-2 participates directly in priming and possibly in fusion steps of Ca2+-triggered vesicle exocytosis. High concentration nanodomains of PI(4,5)P-2 reside on the plasma membrane of neuroendocrine cells. A subset of vesicles that co-localize with PI(4,5)P-2 domains appear to undergo preferential exocytosis in stimulated cells. PI(4,5)P-2 directly regulates vesicle exocytosis by recruiting and activating PI(4,5)P-2-binding proteins that regulate SNARE protein function including CAPS, Munc13-1/2, synaptotagmin-1, and other C2 domain-containing proteins. These PI(4,5)P-2 effector proteins are coincidence detectors that engage in multiple interactions at vesicle exocytic sites. The SNARE protein syntaxin-1 also binds to PI(4,5)P-2, which promotes clustering, but an activating role for PI(4,5)P-2 in syntaxin-1 function remains to be fully characterized. Similar principles underlie polarized constitutive vesicle fusion mediated in part by the PI(4,5)P-2-binding subunits of the exocyst complex (Sec3, Exo70). Overall, focal vesicle exocytosis occurs at sites landmarked by PI(4,5)P-2, which serves to recruit and/or activate multifunctional PI(4,5)P-2-binding proteins. This article is part of a Special Issue entitled Phosphoinositides. (C) 2014 Elsevier B.V. All rights reserved.
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