PIP2Clustering: From model membranes to cells

被引：32
作者：
Brown, Deborah A. [1 ]
机构：
[1] SUNY Stony Brook, Dept Biochem & Cell Biol, Stony Brook, NY 11794 USA
来源：
CHEMISTRY AND PHYSICS OF LIPIDS | 2015年 / 192卷
关键词：
PIP2; Polybasic domain; Exocytosis; Endocytosis; C-KINASE SUBSTRATE; INOSITOL POLYPHOSPHATE 5-PHOSPHATASES; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; PHOSPHOINOSITIDE METABOLISM; PHYSIOLOGICAL FUNCTIONS; ACTIN DYNAMICS; BAR DOMAINS; I-GAMMA; PROTEIN; PIP2;
D O I：
10.1016/j.chemphyslip.2015.07.021
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Phosphoinositides, derived from phosphorylation of phosphatidylinositol at one or more positions on the inositol ring, are minor but significant lipids in eukaryotic cell membranes. Phosphatidylinositol (4,5)-bisphosphate (PIP2) is the most abundant phosphoinositide and is concentrated in the plasma membrane. PIP2 functions in cell motility, adhesion, exocytosis, and endocytosis, among other processes. Model membrane studies have shown that PIP2 can form electrostatic-based clusters with Ca++ and with basic peptides. Recent studies in cells have shown that PIP2 can co-cluster with polybasic peptides present in cellular proteins as well, with important functional consequences. (C) 2015 Elsevier Ireland Ltd. All rights reserved.
引用
收藏
页码：33 / 40
页数：8
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