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J Biol Chem, Vol. 274, Issue 21, 14823-14830, May 21, 1999

Identification of the Ubiquitin Carrier Proteins, E2s, Involved in Signal-induced Conjugation and Subsequent Degradation of Ikappa Balpha

Hedva GonenDagger , Beatrice BercovichDagger , Amir OrianDagger , Andrea Carrano, Chizuko Takizawaparallel , Koji Yamanakaparallel , Michele Pagano, Kazuhiro Iwaiparallel , and Aaron CiechanoverDagger

From the Dagger  Department of Biochemistry and the Rappaport Family Institute for Research in the Medical Sciences, Bruce Rappaport Faculty of Medicine, Haifa 31096, Israel, the  Department of Pathology and the Kaplan Comprehensive Cancer Center, New York University Medical Center, New York, New York 10016, and the parallel  Department of Immunology and Cell Biology, Graduate School of Medicine, Kyoto University, Sankyo-ku, Kyoto 606-8501, Japan

The last step in the activation of the transcription factor NF-kappa B is signal-induced, ubiquitin- and proteasome-mediated degradation of the inhibitor Ikappa Balpha . Although most of the components involved in the activation and degradation pathways have been identified, the ubiquitin carrier proteins (E2) have remained elusive. Here we show that the two highly homologous members of the UBCH5 family, UBCH5b and UBCH5c, and CDC34/UBC3, the mammalian homolog of yeast Cdc34/Ubc3, are the E2 enzymes involved in the process. The conjugation reaction they catalyze in vitro is specific, as they do not recognize the S32A,S36A mutant species of Ikappa Balpha that cannot be phosphorylated and conjugated following an extracellular signal. Furthermore, the reaction is specifically inhibited by a doubly phosphorylated peptide that spans the ubiquitin ligase recognition domain of the inhibitor. Cys-to-Ala mutant species of the enzymes that cannot bind ubiquitin inhibit tumor necrosis factor alpha -induced degradation of the inhibitor in vivo. Not surprisingly, they have a similar effect in a cell-free system as well. Although it is clear that the E2 enzymes are not entirely specific to Ikappa Balpha , they are also not involved in the conjugation and degradation of the bulk of cellular proteins, thus exhibiting some degree of specificity that is mediated probably via their association with a defined subset of ubiquitin-protein ligases. The mechanisms that underlie the involvement of two different E2 species in Ikappa Balpha conjugation are not clear at present. It is possible that different conjugating machineries operate under different physiological conditions or in different cells.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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