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MBC in Press, published online ahead of print October 10, 2007
Mol. Biol. Cell 10.1091/mbc.E06-12-1076

A more recent version of this article appeared on December 1, 2007
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Submitted on December 5, 2006
Revised on September 21, 2007
Accepted on October 1, 2007

The Phosphorylation of Myosin II at the Ser1 and Ser2 Is Critical for Normal PDGF-induced Reorganization of Myosin Filaments

Satoshi Komatsu and Mitsuo Ikebe

Department of Physiology, University of Massachusetts Medical School, Worcester, MA 01655

Monitoring Editor: Paul Forscher

Phosphorylation of the regulatory light chain of myosin II (MLC20) at the activation sites promotes both the motor activity and the filament formation of myosin II thus playing an important role in various cell motile processes. In contrast, the physiological function of phosphorylation of MLC20 at the inhibitory sites is unknown. Here we report for the first time the function of the inhibitory site phosphorylation in the cells. We successfully produced the antibodies specifically recognizing the phosphorylation sites of MLC20 at Ser1, and the platelet-derived growth factor (PDGF)-induced change in the phosphorylation at the Ser1 was monitored. The phosphorylation of MLC20 at the Ser1 significantly increased during the PDGF-induced actin cytoskeletal reorganization. PDGF disassembled the stress fibers, and this was attenuated with the expression of unphosphorylatable MLC20 at the Ser1/Ser2 phosphorylation sites. The present results suggest that the down-regulation of myosin II activity achieved by the phosphorylation at the Ser1/Ser2 sites plays an important role in the normal reorganization of actomyosin filaments triggered by PDGF receptor stimulation.

Address correspondence to: Satoshi Komatsu (satoshi.komatsu{at}umassmed.edu) or Mitsuo Ikebe (mitsuo.ikebe{at}umassmed.edu)




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H. Tanaka, K. Homma, H. D. White, T. Yanagida, and M. Ikebe
Smooth Muscle Myosin Phosphorylated at Single Head Shows Sustained Mechanical Activity
J. Biol. Chem., June 6, 2008; 283(23): 15611 - 15618.
[Abstract] [Full Text] [PDF]


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