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Lookup NU author(s): Dr Lianxi Yang,
Dr Kehinde Ross
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NF-κB-IκB complex formation regulates the level and specificity of NF-κB activity. Quantitative analyses showed that RelA-NF-κB-induced IκBα binding is regulated through inhibitor retention and phosphorylation. RelA caused an increase in IκBα phosphorylation and in degradation, which was enhanced monotonically with inhibitor concentration. In vivo analysis demonstrated the RelA-induced IκBα/RelA interactions to be specific, saturable, and phosphorylation-dependent. In addition, it showed that phosphorylation regulates both the level and affinity of the complexes and demonstrated an increased average affinity to coincide with reduction in the level of complexes during cytokine-induced pathway activation. The data show that RelA regulation of NF-κB-IκBα complex formation is IκBα phosphorylation-dependent and that IκBα/NF-κB binding is dynamic and determined by concentration of the subunits. In addition, they suggest that regulation of both complex levels and affinities through phosphorylation, with effects on the system steady state, participate in selective activation of the NF-κB pathway.
Author(s): Ross K; Yang L; Qwarnstrom EE
Publication type: Article
Publication status: Published
Journal: Journal of Biological Chemistry
ISSN (print): 0021-9258
ISSN (electronic): 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology, Inc.
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