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M510954200v1
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Papers In Press, published online ahead of print March 30, 2006
J. Biol. Chem, 10.1074/jbc.M510954200
Submitted on October 6, 2005
Revised on March 29, 2006
Accepted on March 30, 2006

Nuclear Rho kinase, ROCK2, targets p300 acetyltransferase

Toru Tanaka, Dai Nishimura, Ray-Chan Wu, Mutsuki Amano, Tatsuya Iso, Larry Kedes, Hiroshi Nishida, Kozo Kaibuchi, and Yasuo Hamamori

Medicine, Baylor college of Medicine, Houston, TX 77030

Corresponding Author: hamamori{at}bcm.edu

Rho-associated coiled-coil protein kinase, ROCK, is an effector for the small GTPase Rho, and plays a pivotal role in a diverse array of 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 immuno- fluorescence, 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 nuclear-localized ROCK2 targets p300 for phosphorylation to regulate its acetyl- transferase activity.


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