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J. Biol. Chem., Vol. 281, Issue 22, 15320-15329, June 2, 2006

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Nuclear Rho Kinase, ROCK2, Targets p300 Acetyltransferase^*

Toru Tanaka, Dai Nishimura, Ray-Chang Wu^¶, Mutsuki Amano^||, Tatsuya Iso, Larry Kedes^**, Hiroshi Nishida, Kozo Kaibuchi^||, and Yasuo Hamamori¹

From the Department of Medicine and Center for Cardiovascular Development and the ^¶Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030, the ^||Department of Cell Pharmacology and Institute for Advanced Research, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan, the Department of Medicine and Biological Science, Gunma University School of Medicine, Maebashi 371-8511, Japan, the ^**Departments of Biochemistry and Molecular Biology, and Medicine, Institute for Genetic Medicine, Keck School of Medicine of the University of Southern California, Los Angeles, California 90089-9075, and the Niigata University of Pharmacy and Applied Life Sciences, 265-1 Higashijima, Niigata 956-8603, Japan

Rho-associated coiled-coil protein kinase (ROCK) is an effector for the small GTPase Rho and plays a pivotal role in diverse cellular activities, including cell adhesion, cytokinesis, and gene expression, primarily through an alteration of actin cytoskeleton dynamics. Here, we show that ROCK2 is localized in the nucleus and associates with p300 acetyltransferase both in vitro and in cells. Nuclear ROCK2 is present in a large protein complex and partially cofractionates with p300 by gel filtration analysis. By immunofluorescence, ROCK2 partially colocalizes with p300 in distinct insoluble nuclear structures. ROCK2 phosphorylates p300 in vitro, and nuclear-restricted expression of constitutively active ROCK2 induces p300 phosphorylation in cells. p300 acetyltransferase activity is dependent on its phosphorylation status in cells, and p300 phosphorylation by ROCK2 results in an increase in its acetyltransferase activity in vitro. These observations suggest that nucleus-localized ROCK2 targets p300 for phosphorylation to regulate its acetyltransferase activity.

Received for publication, October 6, 2005 , and in revised form, March 29, 2006.

^* This work was supported in part by Grant 3609 American Heart Association, Texas affiliate, Grant 0455058Y, Muscular Dystrophy Association (to Y. H.), and by the Naito Foundation (to T.T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Center for Cardiovascular Development, Departments of Medicine and Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, 506D, Houston, TX 77030. Tel.: 713-798-3088; Fax: 713-798-7437; E-mail: hamamori{at}bcm.edu.

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