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Abstract
Nuclear factor-kappaB (NF-kappaB) is a transcription factor that has crucial roles
in inflammation, immunity, cell proliferation and apoptosis. Activation of NF-kappaB
mainly occurs via IkappaB kinase (IKK)-mediated phosphorylation of inhibitory molecules,
including IkappaBalpha. Optimal induction of NF-kappaB target genes also requires
phosphorylation of NF-kappaB proteins, such as p65, within their transactivation domain
by a variety of kinases in response to distinct stimuli. Whether, and how, phosphorylation
modulates the function of other NF-kappaB and IkappaB proteins, such as B-cell lymphoma
3, remains unclear. The identification and characterization of all the kinases known
to phosphorylate NF-kappaB and IkappaB proteins are described here. Because deregulation
of NF-kappaB and IkappaB phosphorylations is a hallmark of chronic inflammatory diseases
and cancer, newly designed drugs targeting these constitutively activated signalling
pathways represent promising therapeutic tools.