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Cofilin Phosphorylation and Actin Cytoskeletal Dynamics Regulated by Rho and Cdc42-activated LIM-kinase 2

Cofilin Phosphorylation and Actin Cytoskeletal Dynamics Regulated by Rho and Cdc42-activated LIM-kinase 2,10.1083/jcb.147.7.1519,Journal of Cell Biolo

Cofilin Phosphorylation and Actin Cytoskeletal Dynamics Regulated by Rho and Cdc42-activated LIM-kinase 2   (Citations: 118)
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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 ac- tin 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 (LIMK2/KD) were respec- tively expressed in cells, LIMK2, but not LIMK2/KD, phosphorylated cofilin and induced formation of stress fibers and focal complexes. LIMK2 activity toward cofi- lin phosphorylation was stimulated by coexpression of activated Rho and Cdc42, but not Rac. Importantly, ex- pression of activated Rho and Cdc42, respectively, in- duced stress fibers and filopodia, whereas both Rho- induced stress fibers and Cdc42-induced filopodia were abrogated by the coexpression of LIMK2/KD. In con- trast, the coexpression of LIMK2/KD with the acti- vated Rac did not affect Rac-induced lamellipodia for- mation. These results indicate that LIMK2 plays a crucial role both in Rho- and Cdc42-induced actin cy- toskeletal reorganization, at least in part by inhibiting the functions of cofilin. Together with recent findings that LIMK1 participates in Rac-induced lamellipodia formation, LIMK1 and LIMK2 function under control of distinct Rho subfamily GTPases and are essential regulators in the Rho subfamilies-induced actin cyto- skeletal reorganization.
Journal: Journal of Cell Biology - J CELL BIOL , vol. 147, no. 7, pp. 1519-1532, 1999
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