Definition |
A protein with core domain architecture consisting of an N-terminal Protein kinase domain (Pfam:PF00069), and a C-terminus that is involved in the interaction with NEMO (PR:000001752). In response to a large variety of stimuli, among them pro-inflammatory cytokines, growth factors and microbial pathogens, signals emanating from cell surface receptors converge at the IkappaB kinase (IKK) complex. This complex is composed of four subunits, IKKalpha, IKKbeta, ELK, and NEMO. IKKbeta and NEMO subunits are known to be essential for activating NF-kappaB. Activation of NF-kappaB dimers is the result of IKK-mediated, phosphorylation-induced degradation of the IkappaB inhibitor, which enables the NF-kappaB dimers to enter the nucleus and activate specific target gene expression.
[PIRSF:PIRSF000581, PMID:10359587, PMID:18462684, PRO:CNA]
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