4.6 Article

The carboxy-terminal pleckstrin homology domain of ROCK interacts with filamin-A

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ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0006-291X(03)00048-2

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ROCK/Rho-kinase; filamin-A; actin-binding protein; pleckstrin homology (PH) domain; actin cytoskeleton

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The small GTPase Rho and its effector ROCK/Rho-kinase regulate actin cytoskeletal reorganization through phosphorylation of the regulatory light chain of myosin II. We previously reported that ROCK co-purified with the actin-binding protein filamin-A from HeLa cells. Here, we show that the pleckstrin homology (PH) domain of ROCK, but not the kinase or coiled-coil domain, interacts with filamin-A. We also determined that the PH domain of ROCK binds to the carboxy-terminal region of filamin-A containing the last 24th repeat. ROCK co-localized with filamin-A at the protrusive cell membranes of HeLa cells. (C) 2003 Elsevier Science (USA). All rights reserved.

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