Differential regulation of NF-kappaB2(p100) processing and control by amino-terminal sequences.
作者： J C Betts , G J Nabel
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摘要: Proteolytic degradation of the C-terminal region NF-(kappa)B precursors to their active DNA binding forms represents an important regulatory step in activation NF-(kappa)B. NF-(kappa)B2(p100) is found ubiquitously cytoplasm; however, site and mechanism processing p52 have not previously been defined. We show by deletion mapping that terminates at alanine 405 generate prevented specific inhibitors multicatalytic proteinase complex. Although I(kappa)B-like domain was constitutively phosphorylated, disruption this phosphorylation mutagenesis demonstrated it required as a signal mediate processing. Mutational analysis further showed cleavage NF-(kappa)B2 dependent on sequence motif adjacent 405, ankyrin repeats, or other sequences but directed structural determinants amino terminal site, within Rel homology and/or glycine hinge region. The level much lower than NF-(kappa)B1(p105) differed from I(kappa)B-alpha, suggesting differential control NF-(kappa)B/I(kappa)B family members.
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