| Literature DB >> 21730760 |
Abstract
Transcriptional co-activator p300, which contains an intrinsic histone acetyltransferase activity, is required for an array of important cellular processes. Tight control of p300 function is critical to ensure precise histone acetylation and gene activation. Dysregulation of p300 has been implicated in many types of diseases and numerous studies have examined the functional requirement of p300 to act as a co-activator or as an acetyltransferase for other transcription regulators. Few, however, have tackled how p300 itself is regulated and if posttranslational modification and spatial distribution are means of p300 regulation. In this article, we present a current view on the molecular mechanisms by which the activity and stability of p300 is regulated.Entities:
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Year: 2011 PMID: 21730760 DOI: 10.4161/epi.6.8.16065
Source DB: PubMed Journal: Epigenetics ISSN: 1559-2294 Impact factor: 4.528