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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 and Kozo Kaibuchi
New Series, Vol. 273, No. 5272 (Jul. 12, 1996), pp. 245-248
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/2890422
Page Count: 4
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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.
Science © 1996 American Association for the Advancement of Science