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Various stimuli induce the phosphorylation (
) and subsequent polyubiquitination (
) of IκBs, which are then targeted for degradation by the 26 S proteasome. Associated NF-κB dimers are thereby released to translocate into the nucleus, where they bind to the promoter regions of NF-κB-responsive genes to modulate their expression. The transactivating capacity of nuclear NF-κB dimers can also be regulated by phosphorylation.
