Letter abstract
Nature Cell Biology 8, 509 - 515 (2006)
Published online: 9 April 2006 | doi:10.1038/ncb1402
A ubiquitin-interacting motif protects polyubiquitinated Met4 from degradation by the 26S proteasome
Karin Flick1, Shahri Raasi2,3, Hongwei Zhang1, James L. Yen1 & Peter Kaiser1
Covalent attachment of ubiquitin to proteins regulates a host of cellular events by proteolysis dependent and independent mechanisms. A variety of protein domains that bind non-covalently to ubiquitin have been described and functionally linked to diverse cellular processes1. Overall, however, the understanding and knowledge of the mechanisms by which ubiquitin-binding domains (UBDs) regulate these processes is limited. Here, we describe identification of a UBD in the yeast transcription factor Met4. Met4 activity, but not its stability, is regulated by polyubiquitination2, 3, 4. We found that the UBD restricts the length of the polyubiquitin chain that is assembled on Met4, and prevents proteasomal recognition and degradation of polyubiquitinated Met4. Inactivation of the UBD allowed synthesis of longer ubiquitin chains on Met4 and transformed the normally stable polyubiquitinated Met4 into a short-lived protein. Our results demonstrate a function for UBDs in ubiquitin-chain synthesis and regulation of protein degradation.
- University of California Irvine, Department of Biological Chemistry, School of Medicine, 240D Med Sci I, Irvine, CA 92697-1700, USA.
- Johns Hopkins University, Department of Biochemistry and Molecular Biology, 615 North Wolfe Street, Baltimore, MD 21205, USA.
- Present address: Department of Biology, University of Konstanz, Box M6492, 78457 Konstanz, Germany.
Correspondence to: Peter Kaiser1 e-mail: pkaiser@uci.edu
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