I kappa B epsilon, a novel member of the I kappa B family, controls RelA and cRel NF-kappa B activity.

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阅读量：

103

作者：

Whiteside，T S.

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摘要：

Top of pageIntroduction Results Discussion Materials and methods Acknowledgements References We have isolated a human cDNA which encodes a novel IκB family member using a yeast two-hybrid screen for proteins able to interact with the p52 subunit of the transcription factor NF-κB. The protein is found in many cell types and its expression is up-regulated following NF-κB activation and during myelopoiesis. Consistent with its proposed role as an IκB molecule, IκB- is able to inhibit NF-κB-directed transactivation via cytoplasmic retention of rel proteins. IκB- translation initiates from an internal ATG codon to give rise to a protein of 45 kDa, which exists as multiple phosphorylated isoforms in resting cells. Unlike the other inhibitors, it is found almost exclusively in complexes containing RelA and/or cRel. Upon activation, IκB- protein is degraded with slow kinetics by a proteasome-dependent mechanism. Similarly to IκB-α and IκB-β, IκB- contains multiple ankyrin repeats and two conserved serines which are necessary for signal-induced degradation of the molecule. A unique lysine residue located N-terminal of the serines appears to be not strictly required for degradation. Unlike IκB-α and IκB-β, IκB- does not contain a C-terminal PEST-like sequence. IκB- would, therefore, appear to regulate a late, transient activation of a subset of genes, regulated by RelA/cRel NF-κB complexes, distinct from those regulated by other IκB proteins.

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关键词：

cRel IκB-ϵ protein NF-κB activity RelA

DOI：

10.1093/emboj/16.6.1413

被引量：

816

年份：

1997