Redox-sensitive cellular proteins

Redox-sensitive cellular proteins represent a broad class of proteins that undergo reversible or irreversible structural and functional changes in response to fluctuations in the cellular redox environment. These proteins typically contain highly reactive amino acid residues, most notably cysteine thiols, which serve as sensors for reactive oxygen species (ROS) and reactive nitrogen species (RNS) (PMID: 2842150). Upon modification, these 'redox switches' regulate critical cellular processes including signal transduction, gene expression, and metabolic flux to maintain redox homeostasis (PMID: 30234630). Prominent examples include the transcription factor Nrf2 and its inhibitor Keap1, which coordinate the antioxidant response, as well as various kinases (e.g., ASK1) and phosphatases (e.g., PTEN) that control cell growth and apoptosis (PMID: 21606595). In many diseases, such as cancer and neurodegeneration, the dysregulation of these proteins leads to chronic oxidative stress or aberrant survival signaling. Consequently, they are major focal points for drug development, with therapies like dimethyl fumarate and bardoxolone methyl designed to modulate specific redox-sensitive pathways to treat inflammatory and metabolic conditions (PMID: 23426394, PMID: 31558488).

Other names

Redox-sensitive proteinsThiol-sensitive proteinsOxidative stress-responsive proteinsRedox-regulated proteins

Modulation of reactive amino acid residues, primarily cysteine thiols, through oxidation, reduction, or covalent modification to alter protein conformation, stability, and enzymatic activity, thereby regulating downstream signaling pathways such as the Nrf2-mediated antioxidant response (PMID: 2842150, PMID: 30234630).