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Function and regulation of Cullin-RING ubiquitin ligases

Petroski, Matthew D. and Deshaies, Raymond J. (2005) Function and regulation of Cullin-RING ubiquitin ligases. Nature Reviews. Molecular Cell Biology, 6 (1). pp. 9-20. ISSN 1471-0072. https://resolver.caltech.edu/CaltechAUTHORS:20150318-153239947

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Abstract

Cullin–RING complexes comprise the largest known class of ubiquitin ligases. Owing to the great diversity of their substrate-receptor subunits, it is possible that there are hundreds of distinct cullin–RING ubiquitin ligases in eukaryotic cells, which establishes these enzymes as key mediators of post-translational protein regulation. In this review, we focus on the composition, regulation and function of cullin–RING ligases, and describe how these enzymes can be characterized by a set of general principles.


Item Type:Article
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URLURL TypeDescription
http://dx.doi.org/10.1038/nrm1547 DOIArticle
http://www.nature.com/nrm/journal/v6/n1/full/nrm1547.htmlPublisherArticle
http://www.nature.com/nrm/journal/v6/n1/suppinfo/nrm1547.htmlPublisherSupplementary Information
http://rdcu.be/clP8PublisherFree ReadCube access
ORCID:
AuthorORCID
Deshaies, Raymond J.0000-0002-3671-9354
Additional Information:© 2005 Nature Publishing Group. We thank C.-T. Chien, M. Estelle, E. Kipreos, M. Pagano and D. Wolf for their help with the online supplementary information S2 (table). We also thank G. Kleiger for preparing figure 2. M.D.P. is a postdoctoral fellow and R.J.D. is an assistant investigator of the Howard Hughes Medical Institute, which supports their work.
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Howard Hughes Medical Institute (HHMI)UNSPECIFIED
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Record Number:CaltechAUTHORS:20150318-153239947
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150318-153239947
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:55905
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:18 Mar 2015 23:41
Last Modified:03 Oct 2019 08:09

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