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J Biol Chem, Vol. 273, Issue 52, 35201-35207, December 25, 1998

Degradation of Proto-oncoprotein c-Rel by the Ubiquitin-Proteasome Pathway

Eying ChenDagger , Radmila Hrdlickova§, Jiri Nehyba§, Dan L. Longoparallel , Henry R. Bose Jr.§, and Chou-Chi H. LiDagger

From the Dagger  Intramural Research Support Program, SAIC Frederick, NCI-Frederick Cancer Research and Development Center, Frederick, Maryland 21702, the § Department of Microbiology and Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78712, and the parallel  NIA, National Institutes of Health, Gerontology Research Center, Baltimore, Maryland 21224

The c-rel proto-oncogene product, c-Rel, belongs to the Rel/NF-kappa B transcription factor family, which regulates a large variety of cellular functions. The activation of NF-kappa B involves the degradation of the inhibitor, Ikappa B, through the ubiquitin-proteasome (Ub-Pr)-mediated pathway. Here we report that the turnover of c-Rel is also regulated by the Ub-Pr pathway, thus adding another level of complexity to the regulation of NF-kappa B. High molecular weight ubiquitinated c-Rel conjugates are detected in cells and accumulate in cells treated with proteasome inhibitors. In a cell-free in vitro degradation assay, c-Rel is degraded specifically through the Ub-Pr pathway. N-terminally truncated c-Rel is readily degraded, implying the dispensability of N-terminal sequence; in contrast, a series of deletion mutants missing C-terminal sequences display a reduced susceptibility to the degradation. Interestingly, the sequence between residues 118 and 171 of c-Rel, i.e. the region immediately following the c-Rel/v-Rel homology domain, appears to play an important role in mediating ubiquitin conjugation and the subsequent degradation. Together with our previous study showing an elevated tumorigenic potential for C-terminally truncated mutants, our data suggest that the C-terminal domain of c-Rel plays an important role in mediating c-Rel degradation and growth control.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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