期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 281, 期 18, 页码 12521-12525出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M513333200
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资金
- NCI NIH HHS [R01 CA73756] Funding Source: Medline
- NIAID NIH HHS [R01 AI35098] Funding Source: Medline
Phosphorylation of histone H3 protein at serine 10 is an important step in chromatin remodeling during transcriptional transactivation. IkB kinase-alpha (IKK-alpha) and Mitogen- and Stress- activated protein Kinases 1 and 2 (MSK1/2) have been shown to play key roles in the transcriptional regulation of immediate early genes such as c-fos. Interestingly, IKK-alpha and MSK1/2 have also been implicated as histone H3-Ser(10) kinases. In this work, we have shown that MSK1/2 are required for epidermal growth factor (EGF)-induced, but not tumor necrosis factor-induced, histone H3-Ser(10) phosphorylation, both globally and at specific promoters. Consistent with this, MSK1/2 are required for optimal immediate early c-fos transcription in response to EGF potentially through control of both H3-Ser(10) and promoter-associated cAMP-response element-binding protein phosphorylation. Furthermore, MSK1/2 control EGF-induced IKB alpha promoter H3-Ser(10) phosphorylation in the absence of elevated transcription. These studies demonstrate the existence of pathway-specific mechanisms to control histone H3-Ser(10) phosphorylation and gene expression.
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