What's Ub chain linkage got to do with it?

Ikjin Kim, Hai Rao

Research output: Contribution to journalArticle

20 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)pe18
JournalScience's STKE : signal transduction knowledge environment
Volume2006
Issue number330
DOIs
StatePublished - Apr 11 2006

ASJC Scopus subject areas

  • Medicine(all)

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