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

      Science (New York, N.Y.)

      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, Phosphorylation, Point Mutation, Signal Transduction, T-Lymphocytes, Tetradecanoylphorbol Acetate, Transcriptional Activation, Transfection, Tumor Necrosis Factor-alpha

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          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.

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          7878466

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