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MBC in Press, published online ahead of print December 6, 2006
Mol. Biol. Cell 10.1091/mbc.E06-07-0590

A more recent version of this article appeared on February 1, 2007
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Submitted on July 10, 2006
Revised on November 17, 2006
Accepted on November 22, 2006

Regulation of Myosin II Dynamics by Phosphorylation and Dephosphorylation of Its Light Chain in Epithelial Cells

Toshiyuki Watanabe,*{dagger} Hiroshi Hosoya,{ddagger} and Shigenobu Yonemura*

*RIKEN Center for Developmental Biology, 2-2-3 Minatojima-minamimachi, Chuo-ku, Kobe 650-0047, Japan; {dagger}Department of Life Science, Graduate School of Science and Technology, Kobe University, Kobe 657-8501, Japan; {ddagger}Department of Biological Science, Graduate School of Science, Hiroshima University, Higashi-Hiroshima, Hiroshima, 739-8526, Japan

Monitoring Editor: Erika Holzbaur

Nonmuscle myosin II, an actin-based motor protein, plays an essential role in actin cytoskeleton organization and cellular motility. Although phosphorylation of its regulatory light chain (MRLC) is known to be involved in myosin II filament assembly and motor activity in vitro, it remains unclear exactly how MRLC phosphorylation regulates myosin II dynamics in vivo. We established clones of MDCK II epithelial cells expressing MRLC-EGFP or its mutants. Time-lapse imaging revealed that both phosphorylation and dephosphorylation are required for proper dynamics of myosin II. Inhibitors affecting myosin phosphorylation and MRLC mutants indicated that monophosphorylation of MRLC is required and sufficient for maintenance of stress fibers. Diphosphorylated MRLC stabilized myosin II filaments and was distributed locally in regions of stress fibers where contraction occurs, suggesting that diphosphorylation is involved in the spatial regulation of myosin II assembly and contraction. We further found that myosin phosphatase or Zipper-interacting protein kinase localizes to stress fibers depending on the activity of myosin II ATPase.

Address correspondence to: Shigenobu Yonemura (yonemura{at}cdb.riken.jp)




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