Phosphoinositides in the regulation of actin cortex and cell migration

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

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actin Cytoskeleton / metabolism*
  • Actin Cytoskeleton / ultrastructure
  • Cell Membrane / metabolism*
  • Cell Membrane / ultrastructure
  • Cell Movement / genetics*
  • Cell Shape
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism
  • Gene Expression Regulation
  • Humans
  • Inositol Polyphosphate 5-Phosphatases
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism
  • Myosins / genetics
  • Myosins / metabolism
  • PTEN Phosphohydrolase / genetics
  • PTEN Phosphohydrolase / metabolism
  • Phosphatidylinositol 3-Kinases / genetics
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphatidylinositols / metabolism*
  • Phosphoric Monoester Hydrolases / genetics
  • Phosphoric Monoester Hydrolases / metabolism
  • Signal Transduction

Substances

  • Cytoskeletal Proteins
  • Membrane Proteins
  • Microfilament Proteins
  • Phosphatidylinositols
  • ezrin
  • moesin
  • radixin
  • Phosphatidylinositol 3-Kinases
  • Phosphoric Monoester Hydrolases
  • Inositol Polyphosphate 5-Phosphatases
  • PTEN Phosphohydrolase
  • Myosins