CUP Faculty Research

Title

The p38MAPK Inhibitor SB203580 Alleviates Ultraviolet-Induced Phosphorylation at Serine 389 but Not Serine 15 and Activation of p53

Document Type

Article

Publication Date

1-1-1999

Abstract

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.

Comments

Publication Information.

Keller, D., Zeng, X., Li, X., Kapoor, M., Iordanov, M. S., Taya, Y., Lozano, G., Magun, B., & Lu, H. (1999). The p38MAPK inhibitor SB203580 alleviates ultraviolet-induced phosphorylation at serine 389 but not serine 15 and activation of p53. Biochemical and Biophysical Research Communications, 261(2), 464-471. doi:10.1006/bbrc.1999.1023

Published In

Biochemical and Biophysical Research Communications

Source

CU Commons -- Math and Science Department Faculty Research

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