Structural assembly of cullin-RING ubiquitin ligase complexes

Curr Opin Struct Biol. 2010 Dec;20(6):714-21. doi: 10.1016/j.sbi.2010.08.010. Epub 2010 Sep 27.

Abstract

The cullin-RING ubiquitin ligases (CRLs) are the largest family of multi-subunit E3 ligases in eukaryotes, which ubiquitinate protein substrates in numerous cellular pathways. CRLs share a common arched scaffold and a RING domain catalytic subunit, but use different adaptors and substrate receptors to assemble unique E3 machineries. In comparison to the first CRL structure, recent findings have revealed increased complexity in the overall architecture and assembly mode of CRLs, including multi-domain organization, inter-domain flexibility, and subunit dimerization. These features highlight the capacity of CRLs to catalyze protein ubiquitination under distinct cellular contexts and in response to diverse signals. As the first installment of a two-review series, this article will focus on recent advances in our understanding of CRL assembly mechanisms.

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

  • Animals
  • F-Box Proteins / chemistry
  • F-Box Proteins / metabolism
  • Humans
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Ubiquitin-Protein Ligases / chemistry*
  • Ubiquitin-Protein Ligases / metabolism

Substances

  • F-Box Proteins
  • Ubiquitin-Protein Ligases