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Chromatin Regulates CREB Phosphorylation

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Science's STKE  22 Feb 2000:
Vol. 2000, Issue 20, pp. tw1
DOI: 10.1126/stke.2000.20.tw1

cAMP response element-binding protein (CREB) is a transcription factor that is regulated by phosphorylation by protein kinase A (PKA) which leads to a transient burst in transcriptional activation followed by an attenuation phase as CREB is dephosphorylated. The CREB coactivator proteins, as CBP and p300, possess histone acetylase activity, which induces changes in chromatin structure allowing productive assembly of the transcriptional apparatus onto the target promoter. Michael et al. show that the phosphorylation of CREB and transcription of cAMP-responsive genes can be potentiated by inhibitors of histone deacetylase. Histone deacetylase inhibitors prolonged the length of time that CREB remained phosphorylated, which suggests a chromatin-dependent mechanism for transcriptional attenuation. Their data suggests that promoter-bound nucleosomes can block the accessibility of PKA for CREB, which in turn leads to attenuation of the transcriptional activity.

Michael, L.F., Asahara, H., Shulman, A.I., Kraus, W.L., and Montminy, M. (2000) The phosphorylation status of a cyclic AMP-responsive activator is modulated via a chromatin-dependent mechanism. Mol. Cell. Biol. 20: 1596-1603. [Abstract] [Full Text]

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