Publications
In the most simplistic models of NF-kB signaling, transcriptional activity is regulated by sequestration of active NF-kB dimers in the cytoplasm through their interaction with IkB. In reality, the situation is far more complex - NF-kB transcriptional activity is subject to multiple layers of regulation.
p65:p50 heterodimers, the classical NF-kB complex, require inducible post-translational modification in order to efficiently bring about target gene expression. Work in our lab has focused on the interplay of p65 phosphorylation and recruitment of transcriptional co-activators (see figure).
 
Recent work in our lab has shown that PKAc is a p65 kinase. In unstimulated cells PKAc is associated with p65:p50:IkB complexes. In its unphosphorylated state the C-terminal of the p65 interacts with the Rel-homology domain thereby interfering with DNA-binding as well as association with CBP/p300.
PKAc phosphorylates p65 at serine 276 inducing a conformational change that allows the binding of the transcriptional co-activator CBP/p300 and enhancing the DNA binding activity of p65.
 

for an extensive discussion of post-translational regualtion of NF-kB see the references below and chapter 5 in "Handbook of Transcription Factor NF-kappa B"

 
Ghosh Lab