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

Meredith B. Metzger, Jonathan N. Pruneda, Rachel E. Klevit, Allan M. Weissman

Research output: Contribution to journalReview article

248 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)47-60
Number of pages14
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1843
Issue number1
DOIs
StatePublished - Jan 1 2014

Keywords

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

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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