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Sci. STKE, 11 April 2006
Vol. 2006, Issue 330, p. pe18
[DOI: 10.1126/stke.3302006pe18]

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What’s Ub Chain Linkage Got to Do with It?

Ikjin Kim and Hai Rao*

Institute of Biotechnology, Department of Molecular Medicine, University of Texas Health Science Center, San Antonio, TX 78245, USA.

Abstract: Ubiquitination—the covalent conjugation of ubiquitin (Ub) to other cellular proteins—regulates a wide range of cellular processes. Often, multiple Ub molecules are added to the substrate to form a Ub chain. Distinct outcomes have been observed for substrates modified with multi-Ub chains linked through particular lysine residues. However, recent studies suggest that Ub chain linkages may not be the key determinant for substrate fate. Here, we review evidence suggesting that Ub-binding proteins play a pivotal role in determining the outcome of substrate ubiquitination. In fulfilling their functions in proteasome-mediated proteolysis or signaling, Ub receptors link ubiquitinated proteins to downstream molecules through protein-protein interactions. Studies of Ub-binding factors may therefore hold the key to understanding the diverse functions of the Ub molecule.

*Corresponding author. E-mail: raoh{at}uthscsa.edu

Citation: I. Kim, H. Rao, What’s Ub Chain Linkage Got to Do with It? Sci. STKE 2006, pe18 (2006).

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Rad4 Regulates Protein Turnover at a Postubiquitylation Step.
Y. Li, J. Yan, I. Kim, C. Liu, K. Huo, and H. Rao (2010)
Mol. Biol. Cell 21, 177-185
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