NDLI: Is histone acetylation the most important physiological function for CBP and p300?

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Is histone acetylation the most important physiological function for CBP and p300?

Content Provider	Europe PMC
Author	Bedford, David C. Brindle, Paul K.
Copyright Year	2012
Abstract	Protein lysine acetyltransferases (HATs or PATs) acetylate histones and other proteins, and are principally modeled as transcriptional coactivators. CREB binding protein (CBP, CREBBP) and its paralog p300 (EP300) constitute the KAT3 family of HATs in mammals, which has mostly unique sequence identity compared to other HAT families. Although studies in yeast show that many histone mutations cause modest or specific phenotypes, similar studies are impractical in mammals and it remains uncertain if histone acetylation is the primary physiological function for CBP/p300. Nonetheless, CBP and p300 mutations in humans and mice show that these coactivators have important roles in development, physiology, and disease, possibly because CBP and p300 act as network “hubs” with more than 400 described protein interaction partners. Analysis of CBP and p300 mutant mouse fibroblasts reveals CBP/p300 are together chiefly responsible for the global acetylation of histone H3 residues K18 and K27, and contribute to other locus-specific histone acetylation events. CBP/p300 can also be important for transcription, but the recruitment of CBP/p300 and their associated histone acetylation marks do not absolutely correlate with a requirement for gene activation. Rather, it appears that target gene context (e.g. DNA sequence) influences the extent to which CBP and p300 are necessary for transcription.
Journal	Aging
Volume Number	4
PubMed Central reference number	PMC3371760
Issue Number	4
PubMed reference number	22511639
e-ISSN	19454589
DOI	10.18632/aging.100453
Language	English
Publisher	Impact Journals LLC
Publisher Date	2012-04-01
Access Restriction	Open
Rights License	This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Copyright: © 2012 Bedford and Brindle
Subject Keyword	CBP p300 CREBBP EP300 histones acetylation chromatin transcription coactivators epigenetic cancer CREB cyclic AMP
Content Type	Text
Resource Type	Article
Subject	Aging Cell Biology

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