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Biochim Biophys Acta. 2014 Jan;1843(1):47-60. doi: 10.1016/j.bbamcr.2013.05.026. Epub 2013 Jun 6.

RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination.

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  • 1Laboratory of Protein Dynamics and Signaling, Center for Cancer Research, National Cancer Institute, 1050 Boyles Street, Frederick, MD 21702, USA.


RING finger domain and RING finger-like ubiquitin ligases (E3s), such as U-box proteins, constitute the vast majority of known E3s. RING-type E3s function together with ubiquitin-conjugating enzymes (E2s) to mediate ubiquitination and are implicated in numerous cellular processes. In part because of their importance in human physiology and disease, these proteins and their cellular functions represent an intense area of study. Here we review recent advances in RING-type E3 recognition of substrates, their cellular regulation, and their varied architecture. Additionally, recent structural insights into RING-type E3 function, with a focus on important interactions with E2s and ubiquitin, are reviewed. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System. Guest Editors: Thomas Sommer and Dieter H. Wolf.

Published by Elsevier B.V.


Catalysis; Protein degradation; RING finger; U-box; Ubiquitin ligase (E3); Ubiquitin-conjugating enzyme (E2)

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