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

@article{Kimura1996RegulationOM,
  title={Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase)},
  author={Kazushi Kimura and Masaaki Ito and Mutsuki Amano and Kazuyasu Chihara and Yuko Fukata and Masato Nakafuku and Bunpei Yamamori and Jianhua Feng and Takeshi Nakano and Katsuya Okawa and Akihiro Iwamatsu and Kozo Kaibuchi},
  journal={Science},
  year={1996},
  volume={273},
  pages={245 - 248}
}
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… Expand
Phosphorylation of Myosin-Binding Subunit (Mbs) of Myosin Phosphatase by Rho-Kinase in Vivo
TLDR
Results indicate that MBS is phosphorylated by Rho-kinase downstream of Rho in vivo, and suggest that myosin phosphatase and Rho -kinase spatiotemporally regulate the phosphorylation state of RHo-kinases substrates including MLC and ERM family proteins in vivo in a cooperative manner. Expand
Inhibition of myosin light chain kinase by p21-activated kinase.
TLDR
MLCK activity and MLC phosphorylation were decreased, and cell spreading was inhibited in baby hamster kidney-21 and HeLa cells expressing constitutively active PAK1, indicating that MLCK is a target for p21-activated kinases and that PAKs may regulate cytoskeletal dynamics by decreasing M LCK activity. Expand
Regulation of the Association of Adducin with Actin Filaments by Rho-associated Kinase (Rho-kinase) and Myosin Phosphatase*
  • Kazushi Kimura, Y. Fukata, +5 authors K. Kaibuchi
  • Chemistry, Medicine
  • The Journal of Biological Chemistry
  • 1998
TLDR
The results suggest that Rho-kinase and myosin phosphatase regulate the phosphorylated state of adducin downstream of Rho and that the increased phosphorylation ofadducin by Rho -kinase causes the interaction of ad Ducin with actin filaments. Expand
Rho kinase inhibitor HA-1077 prevents Rho-mediated myosin phosphatase inhibition in smooth muscle cells.
TLDR
Direct in vivo evidence that Rho kinase mediates inhibition of myosin phosphatase activity with resultant enhancement of MLC(20) phosphorylation in smooth muscle is provided and the usefulness of HA-1077 is revealed as a Rho Kinase inhibitor. Expand
Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)*
  • M. Amano, Masaaki Ito, +5 authors K. Kaibuchi
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 1996
TLDR
The phosphorylation of MLC by Rho-kinase resulted in the facilitation of the actin activation of myosin ATPase, which may partly account for the mechanism by which Rho regulates cytokinesis, cell motility, or smooth muscle contraction. Expand
Dynamic Regulation of Myosin Light Chain Phosphorylation by Rho-kinase
TLDR
It is predicted that MLC phosphorylation and myosin phosphatase activity exhibit bistability, and that a novel signaling pathway leading to the auto-activation of myOSinosphatase is required for the regulatory system of MLCosphorylation. Expand
Regulation of myosin phosphatase by a specific interaction with cGMP- dependent protein kinase Ialpha.
TLDR
Un Uncoupling of the cGKIalpha-MBS interaction prevents cGMP-dependent dephosphorylation of myosin light chain, demonstrating that this interaction is essential to the regulation of vascular smooth muscle cell tone. Expand
Elongation Factor-1α Is a Novel Substrate of Rho-Associated Kinase
TLDR
The results suggest that the Rho/Rho-kinase pathway regulates the organization of actin cytoskeleton via the phosphorylation of EF-1α. Expand
Regulation of myosin phosphatase through phosphorylation of the myosin-binding subunit in platelet activation.
TLDR
Treatment of intact platelets with 9, 11-epithio-11,12-methano-thromboxane A2 led to a dramatic increase in phosphorylation of MBS and a significant decrease in the activity of myosin phosphatase. Expand
Targeting by myosin phosphatase‐RhoA interacting protein mediates RhoA/ROCK regulation of myosin phosphatase
TLDR
A new member of the myosin phosphatase complex is found that directly binds to both RhoA and the myOSin‐binding subunit of myosIn phosphatases in vitro, and targets the actinomyosin contractile filament in smooth muscle cells. Expand
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TLDR
Activation of Rho may be linked directly to a serine-threonine kinase pathway, and this phosphorylation was blocked by treatment of cells with botulinum C3 exoenzyme. Expand
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The way phosphorylation mediates or modulates the interaction of actin and myosin in both muscle and nonmuscle systems is discussed, including the phosphorylated proteins in other muscles, as well as nonmuscles cells. Expand
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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