LIM kinase and Diaphanous cooperate to regulate serum response factor and actin dynamics

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LIM kinase and Diaphanous cooperate to regulate serum response factor and actin dynamics

The small GTPase RhoA controls activity of serum response factor (SRF) by inducing changes in actin dynamics. We show that in PC12 cells, activation of SRF after serum stimulation is RhoA dependent, requiring both actin polymerization and the Rho kinase (ROCK)-LIM kinase (LIMK)-cofilin signaling pathway, previously shown to control F-actin turnover. Activation of SRF by overexpression of wild-t...

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Regulation of actin dynamics: The LIM kinase connection

A signalling pathway has recently been delineated that connects Rho-family GTPases to the cytoskeleton via LIM kinase and the F-actin depolymerising protein cofilin. The existence of this pathway helps to explain some of the effects of LIM kinase and cofilin in the control of actin dynamics.

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p57Kip2 regulates actin dynamics by binding and translocating LIM-kinase 1 to the nucleus.

p57Kip2 is the only cyclin-dependent kinase (Cdk) inhibitor shown to be essential for mouse embryogenesis. The fact suggests that p57 has a specific role that cannot be compensated by other Cdk inhibitors. LIM-kinase 1 (LIMK-1) is a downstream effector of the Rho family of GTPases that phosphorylates and inactivates an actin depolymerization factor, cofilin, to induce the formation of actin fib...

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Cofilin Phosphorylation and Actin Cytoskeletal Dynamics Regulated by Rho- and Cdc42-Activated Lim-Kinase 2

The rapid turnover of actin filaments and the tertiary meshwork formation are regulated by a variety of actin-binding proteins. Protein phosphorylation of cofilin, an actin-binding protein that depolymerizes actin filaments, suppresses its function. Thus, cofilin is a terminal effector of signaling cascades that evokes actin cytoskeletal rearrangement. When wild-type LIMK2 and kinase-dead LIMK2...

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 2002

ISSN: 1540-8140,0021-9525

DOI: 10.1083/jcb.200203126