| Literature DB >> 26472704 |
Achilles Ntranos1, Patrizia Casaccia2.
Abstract
Bromodomains are evolutionarily highly conserved α-helical structural motifs that recognize and bind acetylated lysine residues. Lysine acetylation is being increasingly recognized as a major posttranslational modification involved in diverse cellular processes and protein interactions and its deregulation has been implicated in the pathophysiology of various human diseases, such as multiple sclerosis and cancer. Bromodomain-containing proteins can have a wide variety of functions, ranging from histone acetyltransferase activity and chromatin remodeling to transcriptional mediation and co-activation. The role of bromodomains in translating a deregulated cell acetylome into disease phenotypes was recently unveiled by the development of small molecule bromodomain inhibitors. This breakthrough discovery highlighted bromodomain-containing proteins as key players of inflammatory pathways responsible for myelin injury and also demonstrated their role in several aspects of myelin repair including oligodendrocyte differentiation and axonal regeneration.Entities:
Keywords: Bromodomains; Lysine acetylation; Multiple sclerosis; Myelin injury; Remyelination
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Year: 2015 PMID: 26472704 PMCID: PMC4841751 DOI: 10.1016/j.neulet.2015.10.015
Source DB: PubMed Journal: Neurosci Lett ISSN: 0304-3940 Impact factor: 3.046