The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B.
摘要：
We demonstrate an essential role for the proteasome complex in two proteolytic processes required for activation of the transcription factor NF-kappa B. The p105 precursor of the p50 subunit of NF-kappa B is processed in vitro by an ATP-dependent process that requires proteasomes and ubiquitin conjugation. The C-terminal region of p105 is rapidly degraded, leaving the N-terminal p50 domain. p105 processing can be blocked in intact cells with inhibitors of the proteasome or in yeast with proteasome mutants. These inhibitors also block the activation of NF-kappa B and the rapid degradation of I kappa B alpha induced by tumor necrosis factor alpha. Thus, the ubiquitin-proteasome pathway functions not only in the complete degradation of polypeptides, but also in the regulated processing of precursors into active proteins.
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关键词：
Animals Humans Cells, Cultured Proteasome Endopeptidase Complex Cysteine Endopeptidases Adenosine Triphosphate Leupeptins DNA-Binding Proteins NF-kappa B Protein Precursors
DOI：
10.1016/S0092-8674(94)90482-0
被引量：
年份：
1994
Elsevier
Taylor & Francis
Wiley
万方医学
dx.doi.org
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