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Originally published In Press as doi:10.1074/jbc.M109619200 on October 30, 2001

J. Biol. Chem., Vol. 277, Issue 2, 1405-1418, January 11, 2002
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RelB Cellular Regulation and Transcriptional Activity Are Regulated by p100*

Nancie J. SolanDagger , Hiroko MiyoshiDagger , Eva M. CarmonaDagger , Gary D. BrenDagger , and Carlos V. PayaDagger §||

From the Departments of Dagger  Immunology and § Experimental Pathology and Laboratory Medicine and the  Division of Infectious Diseases, Mayo Clinic, Rochester, Minnesota 55905

RelB mediates the constitutive nuclear pool of NF-kappa 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 carboxyl-portion of p100 contains a nuclear export signal(s), which is required for effective retrieval of RelB from the nucleus. Finally, overexpression of NF-kappa B-inducing kinase, 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 NF-kappa B-inducing kinase and/or IKKalpha .

* This work was supported by National Institutes of Health Grant R01 AI36076 and the Mayo Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Mayo Clinic, 200 First St. SW, Guggenheim 501, Rochester, MN 55905. Tel.: 507-284-3747; Fax: 507-284-3757; E-mail: paya@mayo.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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