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Papers In Press, published online ahead of print October 30, 2001
J. Biol. Chem, 10.1074/jbc.M109619200
Submitted on October 4, 2001
Revised on October 30, 2001
Accepted on October 29, 2001

RelB cellular regulation and transcriptional activity are regulated by p100

Nancie J. Solan, Hiroko Miyoshi, Gary D. Bren, and Carlos V. Paya

Exp Pathology, Mayo Clinic, Rochester, MN 55905

Corresponding Author: paya{at}mayo.edu

RelB mediates the constitutive nuclear pool of NF-{kapp}B transcriptional activity in myeloid and lymphoid cells, which is believed to be secondary to its weak interaction with the classical NF-kappa B inhibitor proteins, the Ikappa Bs. In other cell types, RelB is located in the cytosol, thus suggesting that RelB is also regulated by an inhibitory protein(s. In this study, it is demonstrated that RelB is associated in the cytosol with p100 but not with Ikappa Balpha , Ikappa Bbeta , Ikappa Bepsilon , nor p105. Its cytosolic control is not affected by stimuli that lead to RelA nuclear translocation, and RelB nuclear localization is prevented by p100, but not by p105 or Ikappa Balpha . Structure function analysis p100-RelB interactions indicates that p100 amino acids 623-900 are required for effective interaction and repression of nuclear translocation and RelB driven NF-kappa B dependent transcription. Moreover, this carboxy-portion of p100 contains a nuclear export signal(s), which is required for effective retrieval of RelB from the nucleus. Finally, overexpression of NIK, a kinase that has recently been shown to induce p100 processing, possibly through IKKalpha activation, causes nuclear translocation of RelB protein. Thus, these studies indicate that p100 is a bone fide inhibitor of RelB and that this transcription factor may be regulated by NIK and/or IKKalpha .


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