| Autor: |
Keller, David, Zeng, Xiaoya, Li, Xiaorong, Kapoor, Mini, Iordanov, Mihail S., Taya, Yoichi, Lozano, Guillermina, Magun, Bruce, Lu, Hua |
| Zdroj: |
Biochemical and Biophysical Research Communications; August 1999, Vol. 261 Issue: 2 p464-471, 8p |
| Abstrakt: |
Phosphorylation of p53 at serine 389 has been shown to be responsive uniquely to UV but not gamma irradiation. This report describes identification of the UV-responsive p38MAPK protein as a serine 389 kinase. The immunoprecipitated p38MAPK from UV-irradiated murine embryonic testicular carcinoma F9 cells phosphorylated the serine 392 residue but not serine 15 of the human p53 protein in vitro and this phosphorylation was inhibited by a p38MAPK-specific chemical inhibitor SB203580. The inhibitor also remarkably alleviated the UV-caused induction and serine 389 but not serine 15 phosphorylation of the murine p53 protein in vivo. Subsequently, this compound suppressed transcriptional activity of p53 and partially retarded UV-induced apoptosis. Moreover, p53 bound to p38 as revealed by immunoprecipitation with anti-p53 antibodies from UV-treated F9 cells. Thus, these results suggest that UV-stimulated p53 phosphorylation at serine 389 is mediated by the stress-responsive p38MAPK. |
| Databáze: |
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