Myosin I links PIP3 signaling to remodeling of the actin cytoskeleton in chemotaxis

Chun Lin Chen, Yu Wang, Hiromi Sesaki, Miho Iijima

Research output: Contribution to journalArticle

Abstract

Class I myosins participate in various interactions between the cell membrane and the cytoskeleton. Several class I myosins preferentially bind to acidic phospholipids, such as phosphatidylserine and phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2], through a tail homology 1 (TH1) domain. Here, we show that the second messenger lipid phosphatidylinositol 3,4,5-trisphosphate (PIP3) binds to the TH1 domain of a subset of Dictyostelium class I myosins (ID, IE, and IF) and recruits them to the plasma membrane. The PIP3-regulated membrane recruitment of myosin I promoted chemotaxis and induced chemoattractant-stimulated actin polymerization. Similarly, PIP3 recruited human myosin IF to the plasma membrane upon chemotactic stimulation in a neutrophil cell line. These data suggest a mechanism through which the PIP3 signal is transmitted through myosin I to the actin cytoskeleton.

Original languageEnglish (US)
JournalScience signaling
Volume5
Issue number209
DOIs
StatePublished - Jan 31 2012

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Myosin I links PIP<sub>3</sub> signaling to remodeling of the actin cytoskeleton in chemotaxis'. Together they form a unique fingerprint.

  • Cite this