reviewAnnual Review of BiochemistryApr 4, 2017Closed access

Ubiquitin Ligases: Structure, Function, and Regulation

Howard Hughes Medical Institute · University of Washington

PubMed
Indexed incrossrefpubmed

Abstract

Ubiquitin E3 ligases control every aspect of eukaryotic biology by promoting protein ubiquitination and degradation. At the end of a three-enzyme cascade, ubiquitin ligases mediate the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to specific substrate proteins. Early investigations of E3s of the RING (really interesting new gene) and HECT (homologous to the E6AP carboxyl terminus) types shed light on their enzymatic activities, general architectures, and substrate degron-binding modes. Recent studies have provided deeper mechanistic insights into their catalysis, activation, and regulation. In this review, we summarize the current progress in structure-function studies of ubiquitin ligases as…

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1,490
total citations
FWCI
38.57
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100%
References
213
Citations per year

Authors

2

Topics & keywords

Keywords
  • Ubiquitin
  • Ubiquitin-Protein Ligases
  • Ubiquitin ligase
  • Degron
  • Ubiquitin-conjugating enzyme
  • Cell biology
  • Substrate specificity
  • Function (biology)
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