Redox control of protein degradation

• Proteins undergo reversible and irreversible redox modifications.
• Oxidized proteins are cleared mainly through the 20S proteasome and autophagy.
• The proteolytic systems exhibit a dynamic crosstalk to adapt to redox alterations.
• Protein oxidation together with impaired degradation are linked to neurodegeneration.

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.

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