Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

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
Science
New Series, Vol. 273, No. 5272 (Jul. 12, 1996), pp. 245-248
Stable URL: http://www.jstor.org/stable/2890422
Page Count: 4
  • More info
  • Cite this Item
Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho- Kinase)
Preview not available

Abstract

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.

Page Thumbnails

  • Thumbnail: Page 
245
    245
  • Thumbnail: Page 
246
    246
  • Thumbnail: Page 
247
    247
  • Thumbnail: Page 
248
    248