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

Kimura, Kazushi, Ito, Masaaki, Amano, Mutsuki, Chihara, Kazuyasu, Fukata, Yuko, Nakafuku, Masato, Yamamori, Bunpei, Feng, Jianhua, Nakano, Takeshi, Okawa, Katsuya, Iwamatsu, Akihiro, Kaibuchi, Kozo·1996·Science

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.

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Metadata

Authors
Kimura, K., Ito, M., Amano, M., Chihara, K., Fukata, Y., Nakafuku, M., Yamamori, B., Feng, J., Nakano, T., Okawa, K., Iwamatsu, A., & Kaibuchi, K.
Venue
Science
Published
1996-07-12
Volume
273
Issue
5272
Pages
245-248
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2032295238
Cited by
2,884
References
0
FWCI
42.30
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase). https://app.cochat.ai/papers/10.1126/science.273.5272.245
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Kimura, K., Ito, M., Amano, M., Chihara, K., Fukata, Y., Nakafuku, M., Yamamori, B., Feng, J., Nakano, T., Okawa, K., Iwamatsu, A., & Kaibuchi, K. (1996). Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase). Science. https://doi.org/10.1126/science.273.5272.245

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.