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Originally published In Press as doi:10.1074/jbc.M208123200 on November 7, 2002

J. Biol. Chem., Vol. 278, Issue 3, 1594-1602, January 17, 2003
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Proteasomes Modulate Conjugation to the Ubiquitin-like Protein, ISG15*

Mingjuan LiuDagger , Xiao-Ling Li§, and Bret A. HasselDagger §||

From the § Greenebaum Cancer Center,  Department of Microbiology and Immunology, and Dagger  Program in Molecular and Cell Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201

ISG15 is a ubiquitin-like protein that is induced by interferon and microbial challenge. Ubiquitin-like proteins are covalently conjugated to cellular proteins and may intersect the ubiquitin-proteasome system via common substrates or reciprocal regulation. To investigate the relationship between ISG15 conjugation and proteasome function, we treated interferon-induced cells with proteasome inhibitors. Surprisingly, inhibition of proteasomal, but not lysosomal, proteases dramatically enhanced the level of ISG15 conjugates. The stimulation of ISG15 conjugates occurred rapidly in the absence of protein synthesis and was most dramatic in the cytoskeletal protein fraction. Inhibition of ISG15 conjugation by ATP depletion abrogated the proteasome inhibitor-dependent increase in ISG15 conjugates, suggesting that the effect was mediated by de novo conjugation, rather than protection from proteasomal degradation or inhibition of ISG15 deconjugating activity. The increase in ISG15 conjugates did not occur through a stabilization of the ISG15 E1 enzyme, UBE1L. Furthermore, simultaneous modification of proteins by both ISG15 and ubiquitin did not account for the proteasome inhibitor-dependent increase in ISG15 conjugates. These findings provide the first evidence for a link between ISG15 conjugation and proteasome function and support a model in which proteins destined for ISG15 conjugation are proteasome-regulated.

* This work was supported by Grant RPG-99-195-01 from the American Cancer Society (to B. A. H.).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: Greenebaum Cancer Center, University of Maryland School of Medicine, 655 West Baltimore St., 9th Floor BRB, Baltimore, MD 21210. Tel.: 410-328-2344; Fax: 410-328-6559; E-mail: bhassel@som.umaryland.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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