Nuclear Rho Kinase, ROCK2, Targets p300 Acetyltransferase
| Autor: | Ray-Chang Wu, Kozo Kaibuchi, Dai Nishimura, Hiroshi Nishida, Mutsuki Amano, Toru Tanaka, Larry Kedes, Yasuo Hamamori, Tatsuya Iso |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Recombinant Fusion Proteins
Cell Cycle Proteins In Vitro Techniques Protein Serine-Threonine Kinases Biology Peptide Mapping Biochemistry Two-Hybrid System Techniques Animals Humans p300-CBP Transcription Factors ROCK2 Phosphorylation Protein kinase A Cell adhesion Molecular Biology Rho-associated protein kinase Histone Acetyltransferases Cell Nucleus rho-Associated Kinases Binding Sites Effector Intracellular Signaling Peptides and Proteins Cell Biology Actin cytoskeleton Cell biology Multiprotein Complexes Cattle Cytokinesis Transcription Factors |
| Zdroj: | Journal of Biological Chemistry. 281:15320-15329 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m510954200 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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