Identification of p300-targeted acetylated sites in GATA-4 during hypertrophic responses in cardiac myocytes
Tomohide Takaya1, Teruhisa Kawamura1, Tatsuya Morimoto1, Koh Ono2, Toru Kita2, Akira Shimatsu1, Koji Hasegawa1.
- Division of Translational Research, Kyoto Medical Center, National Hospital Organization, Kyoto, Japan.
- Department of Cardiovascular Medicine, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
第11回日本心不全学会学術集会 (千葉), 2007/09/10 (ポスター).
Abstract
A zinc finger protein, GATA-4, is one of the hypertrophy-responsive transcription factors, and increases its DNA-binding and transcriptional activities in response to hypertrophic stimuli in cardiac myocytes. Activation of GATA-4 during this process is mediated, in part, through acetylation by an intrinsic histone acetyltransferase p300. Here, we have identified the most critical lysine residues acting as p300-mediated acetylation targets in GATA-4. By mutational analysis, we found that four lysine residues located at the C-terminal of the first zinc finger domain are required for p300-induced transcriptional activity of GATA-4. A tetra-mutant GATA-4, in which these four lysine residues were simultaneously substituted by alanines, not only showed lack of p300-induced acetylation, DNA-binding and transcriptional activities, but also inhibited transcriptional activation by wild-type GATA-4. Expression of this tetra-mutant GATA-4 in cardiac myocytes specifically inhibited the phenylephrine-induced increase in cell size and myofibrillar organization. Thus, GATA-4 with simultaneous mutation of p300-targeted lysine residues suppresses hypertrophic responses as a dominant-negative form, providing further evidence for the role of the p300/GATA-4 transcriptional pathway in myocardial cell hypertrophy.