The NF-kappa B precursor p105 and the proto-oncogene product Bcl-3 are I kappa B molecules and control nuclear translocation of NF-kappa B.

We have examined the interaction of the NF-kappa B precursor p105 with NF-kappa B subunits. Similar to an I kappa B molecule, p105 associates in the cytoplasm with p50 or p65. Through this assembly, p105 efficiently blocks nuclear transfer of either subunit. Moreover, the p105 protein inhibits DNA binding of ...
dimeric NF-kappa B subunits in a similar, but not identical, manner to its isolated C-terminal domain, which contains an ankyrin-like repeat domain (ARD). The proto-oncogene product Bcl-3 also controls nuclear translocation of p50, but not of p65. Hence, p50 can be retained in the cytoplasm via at least three distinct interactions: through direct interactions either with its own precursor, with Bcl-3 or indirectly through I kappa B alpha or -beta when attached to p65. We discuss a function of p105 as a cytoplasmic assembly unit for homo- and heteromeric NF-kappa B complexes and of Bcl-3 as an I kappa B with novel subunit specificity.
Mesh Terms:
Amino Acid Sequence, Animals, Antibodies, Base Sequence, Cell Nucleus, Cells, Cultured, Cloning, Molecular, DNA-Binding Proteins, Macromolecular Substances, Molecular Sequence Data, Molecular Weight, NF-kappa B, Oligodeoxyribonucleotides, Peptides, Protein Precursors, Proto-Oncogene Proteins, Proto-Oncogenes, Recombinant Proteins, Restriction Mapping, Transcription Factors
EMBO J.
Date: Jan. 01, 1993
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