Control of IκB-α Proteolysis by Site-Specific, Signal-Induced Phosphorylation
- 10 March 1995
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 267 (5203) , 1485-1488
- https://doi.org/10.1126/science.7878466
Abstract
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.Keywords
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