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RING domain E3 ubiquitin ligases

Deshaies, Raymond J. and Joazeiro, Claudio A. P. (2009) RING domain E3 ubiquitin ligases. Annual Review of Biochemistry, 78 . pp. 399-434. ISSN 0066-4154. https://resolver.caltech.edu/CaltechAUTHORS:20090814-114618979

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Abstract

E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate. The activity of most E3s is specified by a RING domain, which binds to an E2~ubiquitin thioester and activates discharge of its ubiquitin cargo. E2-E3 complexes can either monoubiquitinate a substrate lysine or synthesize polyubiquitin chains assembled via different lysine residues of ubiquitin. These modifications can have diverse effects on the substrate, ranging from proteasome-dependent proteolysis to modulation of protein function, structure, assembly, and/or localization. Not surprisingly, RING E3-mediated ubiquitination can be regulated in a number of ways. RING-based E3s are specified by over 600 human genes, surpassing the 518 protein kinase genes. Accordingly, RING E3s have been linked to the control of many cellular processes and to multiple human diseases. Despite their critical importance, our knowledge of the physiological partners, biological functions, substrates, and mechanism of action for most RING E3s remains at a rudimentary stage.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1146/annurev.biochem.78.101807.093809DOIArticle
http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.biochem.78.101807.093809PublisherArticle
ORCID:
AuthorORCID
Deshaies, Raymond J.0000-0002-3671-9354
Additional Information:© 2009 Annual Reviews. We thank Drs. I. Dikic, M. Hochstrasser, B. Schulman, and Y. Ye for providing manuscripts in advance of publication. We also thank Drs. G. Kleiger for Figure 2b, T. Dawson for Figure 15, F. Melchior for discussions, and N. Zheng for comments on the manuscript. R.J.D. is an Investigator of the HHMI, and work on ubiquitin in his lab is supported by HHMI and the NIH. Work on ubiquitin in C.A.P.J.’s lab is supported by grants from the NIH (1 R01 GM083060) and the American Cancer Society (Research Scholar grant 08-298-01-TBE). Our regrets to many colleagues whose work was not cited, especially to document evidence of E3 activity in Supplemental Table 1.
Funders:
Funding AgencyGrant Number
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
NIH1 R01 GM083060
American Cancer Society08-298-01-TBE
Subject Keywords:APC; Cbl; CRL; E2; SCF; UPS
Record Number:CaltechAUTHORS:20090814-114618979
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20090814-114618979
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:15036
Collection:CaltechAUTHORS
Deposited By: Jason Perez
Deposited On:15 Aug 2009 22:14
Last Modified:03 Oct 2019 00:54

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