Published January 2005
| Supplemental Material
Journal Article
Open
Function and regulation of Cullin-RING ubiquitin ligases
- Creators
- Petroski, Matthew D.
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Deshaies, Raymond J.
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.
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.Attached Files
Supplemental Material - nrm1547-S1.pdf
Supplemental Material - nrm1547-S2.pdf
Supplemental Material - nrm1547-S3.pdf
Files
nrm1547-S3.pdf
Additional details
- Eprint ID
- 55905
- Resolver ID
- CaltechAUTHORS:20150318-153239947
- Howard Hughes Medical Institute (HHMI)
- Created
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2015-03-18Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field