cAMP-response Element-binding Protein (CREB) Controls MSK1-mediated Phosphorylation of Histone H3 at the c-fos Promoter in Vitro

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公開日
2010-03-01
資源種別
journal article
権利情報
  • This research was originally published in The journal of biological chemistry. Shimada M; Nakadai T; Fukuda A; Hisatake K. cAMP-response Element-binding Protein (CREB) Controls MSK1-mediated Phosphorylation of Histone H3 at the c-fos Promoter in Vitro. The journal of biological chemistry. 2010. 285:9390-9401. (c) the American Society for Biochemistry and Molecular Biology
DOI
  • 10.1074/jbc.m109.057745
公開者
American Society for Biochemistry and Molecular Biology

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説明

The rapid induction of the c-fos gene correlates with phosphorylations of histone H3 and HMGN1 by mitogen- and stress-activated protein kinases. We have used a cell-free system to dissect the mechanism by which MSK1 phosphorylates histone H3 within the c-fos chromatin. Here, we show that the reconstituted c-fos chromatin presents a strong barrier to histone H3 phosphorylation by MSK1; however, the activators (serum response factor, Elk-1, cAMP-response element-binding protein (CREB), and ATF1) bound on their cognate sites recruit MSK1 to phosphorylate histone H3 at Ser-10 within the chromatin. This activator-dependent phosphorylation of histone H3 is enhanced by HMGN1 and occurs preferentially near the promoter region. Among the four activators, CREB plays a predominant role in MSK1-mediated phosphorylation of histone H3, and the phosphorylation of Ser-133 in CREB is essential for this process. Mutational analyses of MSK1 show that its N-terminal inhibition domain is critical for the kinase to phosphorylate chromatin-embedded histone H3 in a CREB-dependent manner, indicating the presence of an intricate regulatory network for MSK1-mediated phosphorylation of histone H3.

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