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| CENTRAL OF I-KAPPA-B-ALPHA PROTEOLYSIS BY SITE-SPECIFIC, SIGNAL-INDUCED PHOSPHORYLATION |
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| Author(s): BROWN K, GERSTBERGER S, CARLSON L, FRANZOSO G, SIEBENLIST U |
| Source: SCIENCE Volume: 267 Issue: 5203 Pages: 1485-1488 Published: MAR 10 1995 |
| Times Cited: 1,067 References: 19 |
| 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. |
| Document Type: Article |
| Language: English |
Addresses:
1. NIAID, IMMUNOREGULAT LAB, BETHESDA, MD 20892 USA |
| Publisher: AMER ASSOC ADVAN SCIENCE, 1333 H ST NW, WASHINGTON, DC 20005 |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: QL497 |
| ISSN: 0036-8075 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |