Deshaies, R. J. (1999) SCF and Cullin/RING H2-based ubiquitin ligases. Annual Review of Cell and Developmental Biology, 15 . pp. 435-467. ISSN 1081-0706. http://resolver.caltech.edu/CaltechAUTHORS:20120712-093451798
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Protein degradation is deployed to modulate the steady-state abundance of proteins and to switch cellular regulatory circuits from one state to another by abrupt elimination of control proteins. In eukaryotes, the bulk of the protein degradation that occurs in the cytoplasm and nucleus is carried out by the 26S proteasome. In turn, most proteins are thought to be targeted to the 26S proteasome by covalent attachment of a multiubiquitin chain. Ubiquitination of proteins requires a multienzyme system. A key component of ubiquitination pathways, the ubiquitin ligase, controls both the specificity and timing of substrate ubiquitination. This review is focused on a conserved ubiquitin ligase complex known as SCF that plays a key role in marking a variety of regulatory proteins for destruction by the 26S proteasome.
|Additional Information:||© 1999 Annual Reviews. Volume publication date November 1999. I thank Richard Benarous, Zhijian Chen, Kay Hofmann, Peter Jackson, Willy Krek, Matthias Peter, Mike Tyers, and members of my laboratory for providing preprints and communicating unpublished data. I also thank Peter Jackson and Matthias Peter for critical reading of the manuscript. Work on SCF in my laboratory is supported by a grant from the National Institutes of Health, and a Young Investigator Award from the Burroughs-Wellcome Fund.|
|Subject Keywords:||ubiquitin; ubiquitination; F box; Skpl; Cdc34|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Jason Perez|
|Deposited On:||12 Jul 2012 17:12|
|Last Modified:||12 Jul 2012 17:12|
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