Phosphoinositide Regulation of the Actin Cytoskeleton

Helen L. Yin, Paul A. Janmey

Research output: Contribution to journalArticle

523 Citations (Scopus)

Abstract

Phosphoinositides [PPIs, which collectively refer to phosphorylated derivatives of phosphatidylinositol (PI)] have a pivotal role as precursors to important second messengers and as bona fide signaling and scaffold targeting molecules. This review focuses on recent advances that elucidate how PPIs, particularly PI(4,5)P2 (PIP2), directly regulate the actin cytoskeleton in vivo by modulating the activity and targeting of actin regulatory proteins. The role of PIP2 in stimulating actin polymerization and in establishing cytoskeleton-plasma membrane linkages is emphasized. In addition, the review presents tantalizing evidence that suggests how binding of selected cytoskeletal proteins to membrane PPIs may promote PPI clustering into raft lipid microdomains, alter their accessibility to other proteins, and even distort the bilayer conformation. These actions have profound implications for many other PPI-regulated membrane functions that are beginning to be uncovered, and they suggest how PPIs can mediate crosstalk between the actin cytoskeleton and an expanding spectrum of essential cellular functions.

Original languageEnglish (US)
Pages (from-to)761-789
Number of pages29
JournalAnnual Review of Physiology
Volume65
DOIs
StatePublished - 2003

Fingerprint

Phosphatidylinositols
Actin Cytoskeleton
Actins
Cytoskeletal Proteins
Membranes
Second Messenger Systems
Cytoskeleton
Polymerization
Cluster Analysis
Proteins
Cell Membrane
Lipids

Keywords

  • Actin nucleation
  • Actin-membrane linkage
  • Phosphatidylinositol 4,5 bisphosphate

ASJC Scopus subject areas

  • Physiology

Cite this

Phosphoinositide Regulation of the Actin Cytoskeleton. / Yin, Helen L.; Janmey, Paul A.

In: Annual Review of Physiology, Vol. 65, 2003, p. 761-789.

Research output: Contribution to journalArticle

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