Phosphoinositides in the regulation of actin cortex and cell migration

被引:51
作者
Tsujita, Kazuya [1 ]
Itoh, Toshiki [1 ]
机构
[1] Kobe Univ, Biosignal Res Ctr, Org Adv Sci & Technol, Nada Ku, Kobe, Hyogo 6578501, Japan
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 2015年 / 1851卷 / 06期
基金
日本学术振兴会;
关键词
Phosphoinositide; Cortical actin; Adhesion energy; Membrane tension; Cell migration; PLECKSTRIN-HOMOLOGY-DOMAIN; NUCLEOTIDE EXCHANGE FACTOR; PROTEIN TAPP1 INTERACTS; WASP-WIP COMPLEX; MEMBRANE TENSION; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; ERM PROTEINS; N-WASP; NEUTROPHIL CHEMOTAXIS; CYTOSKELETAL ORGANIZATION;
D O I
10.1016/j.bbalip.2014.10.011
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
In order for the cell to function well within a multicellular system, the mechanical properties of the plasma membrane need to meet two different requirements: cell shape maintenance and rearrangement. To achieve these goals, phosphoinositides play key roles in the regulation of the cortical actin cytoskeleton. PI(4,5)P-2 is the most abundant phosphoinositide species in the plasma membrane. It maintains cell shape by linking the actin cortex to the membrane via interactions with Ezrin/Radixin/Moesin (ERM) proteins and class I myosins. Although the role of D3-phosphoinositides, such as PI(3,4,5)P-3, in actin-driven cell migration has been a subject of controversy, it becomes evident that the dynamic turnover of the phosphoinositide by the action of metabolizing enzymes, such as 5-phosphatases, is necessary. Recent studies have revealed an important role of PI(3,4)P-2 in podosome/invadopodia formation, shedding new light on the actin-based organization of membrane structures regulated by phosphoinositide signaling. This article is part of a Special Issue entitled Phosphoinositides. (C) 2014 Elsevier B.V. All rights reserved.
引用
收藏
页码:824 / 831
页数:8
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