Sandbox Reserved 896: Difference between revisions

Human BRD2 protein is a Serine-Threonine kinase found ubiquitously amongst the nuclear envelope of all cell types. The activity of BRD2 is increased during cell proliferation. BRD2 specifically recognizes an N-acetyl-lysine residue at position 12 of histone H4 via a homo-2-mer complex of BD1 domains. The BRD2-BD1 domain recognizes the H4 tail only when lysine-12 is acetylated. This recognition is mediated through the binding of the hypoacetylated side chain of lysine at position 8 of H4 with the interface between dimerized BRD2-BD1 domains [3]. BRD2 has also shown in vitro interaction with N-acetyl-lysine at position 5 of K12, but this interaction has not been shown to involve lysine-8 of H4 [3]. It is presumed that one of the functions of this recognition is to prevent deletion or erasure of post-translational histone markers during the mitotic cell cycle. The transcriptional regulation activity of BRD2 is also mediated through its positive regulation of E2F-dependent cell cycle progression (direct stimulation of E2F reporter activity) [1]. As E2F’s central function is to promote the synthesis of proteins needed for G1 to S transition, BRD2-BD1 is directly implicated in the regulation of the cell cycle.