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Sci. Signal., 31 January 2012
Vol. 5, Issue 209, p. ra10
[DOI: 10.1126/scisignal.2002446]

RESEARCH ARTICLES

Myosin I Links PIP3 Signaling to Remodeling of the Actin Cytoskeleton in Chemotaxis

Chun-Lin Chen*, Yu Wang, Hiromi Sesaki, and Miho Iijima{dagger}

Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

* Present address: Department of Biological Science, National Sun Yat-Sen University, 70 Lien-Hai Road, Kaohsiung, Taiwan 80424, R.O.C.

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.

{dagger} To whom correspondence should be addressed. E-mail: miijima{at}jhmi.edu

Citation: C.-L. Chen, Y. Wang, H. Sesaki, M. Iijima, Myosin I Links PIP3 Signaling to Remodeling of the Actin Cytoskeleton in Chemotaxis. Sci. Signal. 5, ra10 (2012).

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