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Science 12 July 1996:
Vol. 273. no. 5272, pp. 245 - 248
DOI: 10.1126/science.273.5272.245

Reports

Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase)

Kazushi Kimura, Masaaki Ito, Mutsuki Amano, Kazuyasu Chihara, Yuko Fukata, Masato Nakafuku, Bunpei Yamamori, Jianhua Feng, Takeshi Nakano, Katsuya Okawa, Akihiro Iwamatsu, Kozo Kaibuchi *

The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP·RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP·RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase.

K. Kimura, M. Amano, K. Chihara, Y. Fukata, M. Nakafuku, K. Kaibuchi, Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 630-01, Japan.
M. Ito, B. Yamamori, J. Feng, T. Nakano, First Department of Internal Medicine, Mie University School of Medicine, Tsu 514, Japan.
K. Okawa and A. Iwamatsu, Central Laboratories for Key Technology, Kirin Brewery Company Limited, Yokohama 236, Japan.
* To whom correspondence should be addressed.



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H. Matsumoto, L. M Moir, B. G G Oliver, J. K Burgess, M. Roth, J. L Black, and B. E McParland (2007)
Thorax 62, 848-854
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Postnatal maturation modulates relationships among cytosolic Ca2+, myosin light chain phosphorylation, and contractile tone in ovine cerebral arteries.
R. J. Sandoval, E. R. Injeti, W. T. Gerthoffer, and W. J. Pearce (2007)
Am J Physiol Heart Circ Physiol 293, H2183-H2192
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Science. ISSN 0036-8075 (print), 1095-9203 (online)