Function and regulation of cullin–RING ubiquitin ligases

We focus on the composition, regulation and function of cullin–RING ligases, and describe how these enzymes can be characterized by a set of general principles

Matthew D. Petroski; Raymond J. Deshaies


Scholarcy highlights

  • UBIQUITIN LIGASE A protein or protein complex that facilitates the transfer of ubiquitin from the active-site cysteine of a ubiquitinconjugating enzyme to a Lys residue of a substrate
  • There is a great diversity of CULLIN–RING LIGASES in terms of their composition and function, we propose that these enzymes can be characterized by a set of general principles that will apply to most members of the superfamily
  • Substrate receptors have many targets and functions. It remains unclear how many of the human Fbox, suppressor of cytokine signalling/elongin-BC-box and BTB-domain proteins assemble with cullins to form ubiquitin ligases, a survey of the available literature indicates that more than 50 different CRLs assemble in human cells
  • Since the discovery of SCFCdc in 1997, ubiquitin ligases that are based on a cullin–RING catalytic core have moved to centre stage in regulatory biology
  • The structural biology of CRLs is providing key insights into the conserved architecture of this superfamily of enzymes and the chemical basis for their specificity, but has served to highlight how little we know about how these enzymes work
  • Recent research has emphasized the importance of a posttranslational-modification cycle — neddylation — that might control the dynamic equilibrium of CRL assembly and disassembly
  • Progress over the past seven years has been truly impressive, our understanding of the CULLIN–RING LIGASES superfamily of enzymes remains in its infancy

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