Publication Date:
1995-03-10
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, K -- Gerstberger, S -- Carlson, L -- Franzoso, G -- Siebenlist, U -- New York, N.Y. -- Science. 1995 Mar 10;267(5203):1485-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892-1876.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7878466" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Cell Line
;
DNA-Binding Proteins/chemistry/genetics/*metabolism
;
Humans
;
*I-kappa B Proteins
;
Ionomycin/pharmacology
;
Mice
;
Molecular Sequence Data
;
Mutation
;
NF-kappa B/*antagonists & inhibitors/metabolism
;
Phosphorylation
;
Point Mutation
;
Signal Transduction
;
T-Lymphocytes
;
Tetradecanoylphorbol Acetate/pharmacology
;
Transcriptional Activation
;
Transfection
;
Tumor Necrosis Factor-alpha/pharmacology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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