The carboxy-terminal pleckstrin homology domain of ROCK interacts with filamin-A |
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Authors: | Ueda Kozue Ohta Yasutaka Hosoya Hiroshi |
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Affiliation: | Department of Biological Science, Graduate School of Science, Hiroshima University, 739-8526, Higashi-Hiroshima, Japan. |
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Abstract: | 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. |
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Keywords: | ROCK/Rho-kinase Filamin-A Actin-binding protein Pleckstrin homology (PH) domain Actin cytoskeleton |
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