Proteasome substrate receptors and their therapeutic potential

Trends Biochem Sci. 2022 Nov;47(11):950-964. doi: 10.1016/j.tibs.2022.06.006. Epub 2022 Jul 9.

Abstract

The ubiquitin-proteasome system (UPS) is critical for protein quality control and regulating protein lifespans. Following ubiquitination, UPS substrates bind multidomain receptors that, in addition to ubiquitin-binding sites, contain functional domains that bind to deubiquitinating enzymes (DUBs) or the E3 ligase E6AP/UBE3A. We provide an overview of the proteasome, focusing on its receptors and DUBs. We highlight the key role of dynamics and importance of the substrate receptors having domains for both binding and processing ubiquitin chains. The UPS is rich with therapeutic opportunities, with proteasome inhibitors used clinically and ongoing development of small molecule proteolysis targeting chimeras (PROTACs) for the degradation of disease-associated proteins. We discuss the therapeutic potential of proteasome receptors, including hRpn13, for which PROTACs have been developed.

Keywords: deubiquitinating enzymes; proteasome; substrate receptors; ubiquitin.

Publication types

  • Review
  • Research Support, N.I.H., Intramural

MeSH terms

  • Carrier Proteins / metabolism
  • Deubiquitinating Enzymes / metabolism
  • Proteasome Endopeptidase Complex* / metabolism
  • Proteasome Inhibitors*
  • Proteins / metabolism
  • Proteolysis
  • Ubiquitin / metabolism
  • Ubiquitin-Protein Ligases / metabolism
  • Ubiquitination

Substances

  • Carrier Proteins
  • Proteasome Inhibitors
  • Proteins
  • Ubiquitin
  • Ubiquitin-Protein Ligases
  • Deubiquitinating Enzymes
  • Proteasome Endopeptidase Complex