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MBC in Press, published online ahead of print September 13, 2006
Mol. Biol. Cell 10.1091/mbc.E06-05-0449

A more recent version of this article appeared on November 1, 2006
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Submitted on May 23, 2006
Accepted on August 31, 2006

Myo1c Binds Phosphoinositides through a Putative PH Domain

David E. Hokanson,* Joseph M. Laakso,* Tianming Lin,* David Sept,{dagger} and E. Michael Ostap*

*The Pennsylvania Muscle Institute and Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6085; {dagger}Department of Biomedical Engineering and Center for Computational Biology, Washington University, St. Louis, MO 63130

Monitoring Editor: Carole Parent

Myo1c is a member of the myosin superfamily that binds PIP2, links the actin cytoskeleton to cellular membranes, and plays roles in mechano-signal transduction and membrane trafficking. We located and characterized two distinct membrane binding sites within the regulatory and tail domains of this myosin. By sequence, secondary structure, and ab initio computational analyses, we identified a phosphoinositide binding site in the tail to be a putative pleckstrin homology (PH) domain. Point mutations of residues known to be essential for poly-phosphoinositide binding in previously characterized PH domains inhibit myo1c binding to PIP2 in vitro, disrupt in vivo membrane binding, and disrupt cellular localization. The extended sequence of this binding site is conserved within other myosin-I isoforms, suggesting they too contain this putative PH domain. We also characterized a previously identified membrane binding site within the IQ motifs in the regulatory domain. This region is not phosphoinositide specific, but binds anionic phospholipids in a calcium dependent manner. However, this site is not essential for in vivo membrane binding.

Address correspondence to: E. Michael Ostap (ostap{at}mail.med.upenn.edu)




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