Role of unphosphorylated, newly synthesized I kappa B beta in persistent activation of NF-kappa B.

Stimulation with inducers that cause persistent activation of NF-kappa B results in the degradation of the NF-kappa B inhibitors, I kappa B alpha and I kappa B beta. Despite the rapid resynthesis and accumulation of I kappa B alpha, NF-kappa B remains induced under these conditions. We now report that ...
I kappa B beta is also resynthesized in stimulated cells and appears as an unphosphorylated protein. The unphosphorylated I kappa B beta forms a stable complex with NF-kappa B in the cytosol; however, this binding fails to mask the nuclear localization signal and DNA binding domain on NF-kappa B, and the I kappa B beta-NF-kappa B complex enters the nucleus. It appears therefore that during prolonged stimulation, I kappa B beta functions as a chaperone for NF-kappa B by protecting it from I kappa B alpha and allowing it to be transported to the nucleus.
Mesh Terms:
Animals, COS Cells, Cell Nucleus, Cercopithecus aethiops, Cytosol, DNA-Binding Proteins, Electrophoresis, Polyacrylamide Gel, I-kappa B Proteins, Kinetics, Lipopolysaccharides, Models, Structural, NF-kappa B, Phosphorylation, Protease Inhibitors, Recombinant Fusion Proteins, Transfection
Mol. Cell. Biol.
Date: Oct. 01, 1996
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