Our lab has been working on the activation and repression mechanisms by which p53 and AP-1 modulate cellular and viral gene expression via:
functional association with BRD4 and general transcription components.
how posttranslational modifications (methylation, acetylation, sumoylation, neddylation, and ubiquitination) fine-tune the transcriptional activity of these transcription factors via covalent linkage of critical lysine residues.
Reconstituted histone acetyltransferase (HAT) assays and in vitro methylation, phosphorylation, sumoylation, neddylation, and ubiquitination assays are routinely used in the lab to define the role of posttranslational modification in modulating transcription factor activity and various signaling pathways.
We are also interested in:
dissecting the molecular mechanism underlying p300/CBP and G9a/GLP involvement in gene activation and repression by switching its role from activation to repression
how phosphorylation regulates BRD4 chromatin targeting and recruitment of various transcription factors and chromatin modifiers, with concurrent development of phospho-BRD4-targeting compounds to modulate these processes.