Journal
FEBS LETTERS
Volume 586, Issue 17, Pages 2692-2704Publisher
WILEY
DOI: 10.1016/j.febslet.2012.04.045
Keywords
Bromodomain; Lysine acetylation; Sequence specificity
Funding
- Canadian Institutes for Health Research [1097737]
- Canada Foundation for Innovation
- Genome Canada
- GlaxoSmithKline
- Pfizer
- Eli Lilly
- Novartis Research Foundation
- Ontario Ministry of Research and Innovation
- Wellcome Trust
- Wellcome Trust [095751/Z/11/Z]
- Wellcome Trust [095751/Z/11/Z] Funding Source: Wellcome Trust
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epsilon-N-acetylation of lysine residues (K-ac) is one of the most abundant post-translation modifications (PTMs) in the human proteome. In the nucleus, acetylation of histones has been linked to transcriptional activation of genes but the functional consequences of most acetylation events and proteins recruited to these sites remains largely unknown. Bromodomains (BRDs) are small helical interaction modules that specifically recognize acetylation sites in proteins. BRDs have recently emerged as interesting targets for the development of specific protein interaction inhibitors, enabling a novel exiting strategy for the development of new therapies. This review provides an overview over sequence requirements of BRDs, known substrates and the structural mechanisms of specific K-ac recognition. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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