Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation.


I kappa B-alpha inhibits transcription factor NF-kappa B by retaining it in the cytoplasm. Various stimuli, typically those associated with stress or pathogens, rapidly inactivate I kappa B-alpha. This liberates NF-kappa B to translocate to the nucleus and initiate transcription of genes important for the defense of the organism. Activation of NF-kappa B correlates with phosphorylation of I kappa B-alpha and requires the proteolysis of this inhibitor. When either serine-32 or serine-36 of I kappa B-alpha was mutated, the protein did not undergo signal-induced phosphorylation or degradation, and NF-kappa B could not be activated. These results suggest that phosphorylation at one or both of these residues is critical for activation of NF-kappa B.

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@article{Brown1995ControlOI, title={Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation.}, author={Keith D. Brown and Stefanie Gerstberger and Lauren M. Carlson and Guido Franzoso and Ulrich K. Siebenlist}, journal={Science}, year={1995}, volume={267 5203}, pages={1485-8} }