Title : Brd4 coactivates transcriptional activation of NF-kappaB via specific binding to acetylated RelA.

Pub. Date : 2009 Mar

PMID : 19103749






4 Functional Relationships(s)
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1 In this study, we demonstrate that bromodomains of Brd4 bind to acetylated lysine-310. Lysine bromodomain containing 4 Homo sapiens
2 Brd4 enhances transcriptional activation of NF-kappaB and the expression of a subset of NF-kappaB-responsive inflammatory genes in an acetylated lysine-310-dependent manner. Lysine bromodomain containing 4 Homo sapiens
3 Bromodomains of Brd4 and acetylated lysine-310 of RelA are both required for the mutual interaction and coactivation function of Brd4. Lysine bromodomain containing 4 Homo sapiens
4 Our results identify Brd4 as a novel coactivator of NF-kappaB through specifically binding to acetylated lysine-310 of RelA. Lysine bromodomain containing 4 Homo sapiens