P38 MAPK enhances STAT1-dependent transcription independently of Ser-727 phosphorylation.

ABSTRACT: The transcription factor signal transducer and activator of transcription 1 (STAT1) requires phosphorylation at both Tyr-701 and Ser-727 for full activation. IFN-gamma induces phosphorylation of both residues, whereas stress signals like UV or lipopolysaccharide stimulate phosphorylation of Ser-727 only. Using p38alpha mitogen-activated protein kinase (MAPK)-deficient cells, we show that the stress-induced phosphorylation of Ser-727 requires p38alpha MAPK activity, whereas IFN-gamma-stimulated Ser-727 phosphorylation occurs independently of the p38alpha pathway. Consistently, IFN-gamma stimulated expression of the STAT1 target gene IRF1 to a similar extent in both wild-type and p38alpha-deficient cells. However, stress-induced activation of the p38 MAPK pathway considerably enhanced the IF

SUBMITTER: Ramsauer K 

PROVIDER: S-EPMC130550 | biostudies-literature | 2002 Oct

REPOSITORIES: biostudies-literature