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Biochim Biophys Acta. 2015 Jun;1851(6):824-31. doi: 10.1016/j.bbalip.2014.10.011. Epub 2014 Oct 29.

Phosphoinositides in the regulation of actin cortex and cell migration.

Author information

1
Biosignal Research Center, Organization of Advanced Science and Technology, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe, Hyogo 657-8501, Japan. Electronic address: tsujita@people.kobe-u.ac.jp.
2
Biosignal Research Center, Organization of Advanced Science and Technology, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe, Hyogo 657-8501, Japan. Electronic address: titoh@people.kobe-u.ac.jp.

Abstract

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)P₂is 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)P₃, 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)P₂in 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.

KEYWORDS:

Adhesion energy; Cell migration; Cortical actin; Membrane tension; Phosphoinositide

PMID:
25449647
DOI:
10.1016/j.bbalip.2014.10.011
[Indexed for MEDLINE]

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