New insights into ubiquitin E3 ligase mechanism

Nat Struct Mol Biol. 2014 Apr;21(4):301-7. doi: 10.1038/nsmb.2780.

Abstract

E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct classes of E3 ligases have been identified that stimulate transfer of ubiquitin and ubiquitin-like proteins through either a direct or an indirect mechanism. Only recently have the catalytic mechanisms of E3 ligases begun to be elucidated.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Catalysis
  • Lysine / chemistry
  • Lysine / metabolism
  • Models, Biological*
  • Signal Transduction
  • Substrate Specificity
  • Ubiquitin-Conjugating Enzymes / metabolism
  • Ubiquitin-Protein Ligases / chemistry
  • Ubiquitin-Protein Ligases / physiology*
  • Ubiquitination / physiology*
  • Ubiquitins / metabolism

Substances

  • Ubiquitins
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligases
  • Lysine