Redox control of protein degradation

Redox Biol. 2015 Dec:6:409-420. doi: 10.1016/j.redox.2015.07.003. Epub 2015 Sep 9.

Abstract

Intracellular proteolysis is critical to maintain timely degradation of altered proteins including oxidized proteins. This review attempts to summarize the most relevant findings about oxidant protein modification, as well as the impact of reactive oxygen species on the proteolytic systems that regulate cell response to an oxidant environment: the ubiquitin-proteasome system (UPS), autophagy and the unfolded protein response (UPR). In the presence of an oxidant environment, these systems are critical to ensure proteostasis and cell survival. An example of altered degradation of oxidized proteins in pathology is provided for neurodegenerative diseases. Future work will determine if protein oxidation is a valid target to combat proteinopathies.

Keywords: Autophagy; Proteasome; Protein oxidation; Proteolysis; Unfolded protein response.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Alzheimer Disease / genetics
  • Alzheimer Disease / metabolism*
  • Alzheimer Disease / pathology
  • Autophagy / genetics
  • Humans
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Oxidation-Reduction
  • Parkinson Disease / genetics
  • Parkinson Disease / metabolism*
  • Parkinson Disease / pathology
  • Prion Diseases / genetics
  • Prion Diseases / metabolism*
  • Prion Diseases / pathology
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Processing, Post-Translational*
  • Proteolysis
  • Reactive Oxygen Species / metabolism*
  • Ubiquitin / genetics
  • Ubiquitin / metabolism
  • Ubiquitination
  • Unfolded Protein Response / genetics

Substances

  • Nerve Tissue Proteins
  • Reactive Oxygen Species
  • Ubiquitin
  • Proteasome Endopeptidase Complex