RT Journal Article
SR Electronic
T1 Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation
JF Science
JO Science
FD American Association for the Advancement of Science
SP 1485
OP 1488
DO 10.1126/science.7878466
VO 267
IS 5203
A1 Brown, K
A1 Gerstberger, S
A1 Carlson, L
A1 Franzoso, G
A1 Siebenlist, U
YR 1995
UL http://science.sciencemag.org/content/267/5203/1485.abstract
AB 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.