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- PMID: 12514134
- UKPMCID: 12514134
- DOI: 10.1093/emboj/cdg028
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MAP kinase phosphorylation-dependent activation of Elk-1 leads to activation of the co-activator p300.
Li, Qi-Jing; Yang, Shen-Hsi; Maeda, Yutaka; Sladek, Frances M; Sharrocks, Andrew D; Martins-Green, Manuela
The EMBO journal. 2003;22(2):281-91.
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Full-text held externally
- PMID: 12514134
- UKPMCID: 12514134
- DOI: 10.1093/emboj/cdg028
Abstract
CBP/p300 recruitment to enhancer-bound complexes is a key determinant in promoter activation by many transcription factors. We present a novel mechanism of activating such complexes and show that pre-assembled Elk-1-p300 complexes become activated following Elk-1 phosphorylation by changes in Elk-1-p300 interactions rather than recruitment. It is known that Elk-1 binds to promoter in the absence of stimuli. However, it is unclear how activation of Elk-1 by mitogen-acivated protein kinase (MAPK)-mediated phosphorylation leads to targeted gene transactivation. We show that Elk-1 can interact with p300 in vitro and in vivo in the absence of a stimulus through the Elk-1 C-terminus and the p300 N-terminus. Phosphorylation on Ser383 and Ser389 of Elk-1 by MAPK enhances this basal binding but, most importantly, Elk-1 exhibits new interactions with p300. These interaction changes render a strong histone acetyltransferase activity in the Elk-1-associated complex that could play a critical role in chromatin remodeling and gene activation. The pre-assembly mechanism may greatly accelerate transcription activation, which is important in regulation of expression of immediate-early response genes, in particular those involved in stress responses.