A GATA-4 mutant lacking p300-induced acetylation suppresses myocardial cell hypertrophy
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71回日本循環器学会学術集会 (神戸), 2007/03/17 (ポスター).
Abstract
A zinc finger protein GATA-4 is one of 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 i mediated, in part, through acetylation by intrinsic histone acetyltransferase such as a transcriptional coactivator p300. However, GATA-4 acetylation targets by p300 during myocardial cell hypertrophy have not been identified. Within GATA-4, nine lysine residues, possible acetylation sites, exist near the two zinc fingers that serve as cofactor- and DNA-binding domains. By mutational analysis, we have found that four lysine residues located at amino acid sequences between 311-322 are required for synergistic activation of atrial natriuretic factor and endothelin-1 promoters by GATA-4 and p300. A tetra-mutant GATA4, in which these four lysine residues are simultaneously substituted with 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 cultured neonatal cardiac myocytes using a lentivirus vector suppressed phenylephrine-induced increase in cell size and myofibrillar organization. However, the expression did not affect cardiac myocytes at a basal state. Thus, we have identified the most critical lysine residues of p300-mediated acetylation target in GATA-4 and demonstrate that GATA-4 with simultaneous mutation of these sites suppresses hypertrophic responses as a dominant-negative form in cardiac myocytes.