Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in the degradation of IκBα
Copyright policy )Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in the degradation of IκBα
The NF-κB/Rel proteins are sequestered in the cytoplasm in association with IκBα. In response to external signals, IκBα is phosphorylated, multi-ubiquitinated, and degraded by proteasomes, thereby releasing NF-κB/Rel proteins to migrate to the nucleus. We have cloned a mouse ubiquitin-conjugating enzyme (mE2), which associates with IκBα. mE2 is homologous to the yeast Ubc9/Hus5 ubiquitin-conjugating enzyme. A transdominant-negative mutant of mE2 had no effect on phosphorylation of IκBα, but delayed its degradation. Correspondingly, tumor necrosis factor-α-inducible NF-κB activity was diminished. We propose that mE2 is directly involved in the ubiquitin conjugation of IκBα, a pivotal step in its degradation pathway.
- University of California, San Diego United States
- Salk Institute for Biological Studies United States
DNA, Complementary, Base Sequence, Hydrolysis, Molecular Sequence Data, NF-kappa B, Cell Line, DNA-Binding Proteins, Fungal Proteins, Ligases, Mice, NF-KappaB Inhibitor alpha, Mutagenesis, Ubiquitin-Conjugating Enzymes, Animals, I-kappa B Proteins, Amino Acid Sequence, Schizosaccharomyces pombe Proteins, Cloning, Molecular, Genes, Dominant, Protein Binding
DNA, Complementary, Base Sequence, Hydrolysis, Molecular Sequence Data, NF-kappa B, Cell Line, DNA-Binding Proteins, Fungal Proteins, Ligases, Mice, NF-KappaB Inhibitor alpha, Mutagenesis, Ubiquitin-Conjugating Enzymes, Animals, I-kappa B Proteins, Amino Acid Sequence, Schizosaccharomyces pombe Proteins, Cloning, Molecular, Genes, Dominant, Protein Binding
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