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NF-kappaB-inducing kinase regulates the processing of NF-kappaB2 p100.

Molecular cell | Feb 12, 2001

http://www.ncbi.nlm.nih.gov/pubmed/11239468

Processing of the nf(kappa)b2 gene product p100 to generate p52 is an important step in NF-kappaB regulation. We show that this step is negatively regulated by a processing-inhibitory domain (PID) within p100 and positively regulated by the NF-kappaB-inducing kinase (NIK). While the PID suppresses the constitutive processing of p100, NIK induces p100 processing by stimulating site-specific phosphorylation and ubiquitination of this precursor protein. Further, a natural mutation of the gene encoding NIK in alymphoplasia (aly) mice cripples the function of NIK in p100 processing, causing a severe defect in p52 production. These data suggest that NIK is a specific kinase regulating p100 processing and explain why the aly and nf(kappa)b2 knockout mice exhibit similar immune deficiencies.

Pubmed ID: 11239468 RIS Download

Mesh terms: Animals | Binding Sites | Cell Line | Genotype | Humans | Immunoblotting | Mice | Mice, Mutant Strains | Molecular Weight | Mutation | NF-kappa B | NF-kappa B p52 Subunit | Phosphorylation | Phosphoserine | Protein Binding | Protein Processing, Post-Translational | Protein Structure, Tertiary | Protein-Serine-Threonine Kinases | Substrate Specificity | Transfection | Ubiquitins

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Associated grants

  • Agency: NIAID NIH HHS, Id: 1R01 AI45045

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