Nuclear Rho kinase, ROCK2, targets p300 acetyltransferase

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

Research output: Contribution to journalArticlepeer-review

91 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)15320-15329
Number of pages10
JournalJournal of Biological Chemistry
Issue number22
Publication statusPublished - 02-06-2006
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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