ArticleFree radical biology & medicine2016
Peroxiredoxin 6 homodimerization and heterodimerization with glutathione S-transferase pi are required for its peroxidase but not phospholipase A2 activity.
Article in Free radical biology & medicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 64 citations in OpenAlex.
- USP19 facilitates CSE-induced cell damage and ferroptosis in chronic obstructive pulmonary disease by deubiquitinating HDAC6 to drive PRDX6 deacetylation.Immunologic research · 2026Article
- Moonlighting Functions of Mammalian Peroxiredoxins in Cellular Signaling.Antioxidants (Basel, Switzerland) · 2026Review
- Peroxiredoxins in central nervous system: implications for chronic pain and anaesthetic-induced neurotoxicity management.Redox biology · 2025Review
- Role of aspartate 42 and histidine 79 in the aiPLAScientific reports · 2025Article
- Therapeutic prospects and potential mechanisms of Prdx6: as a novel target in musculoskeletal disorders.Frontiers in physiology · 2025Review
- Prdx6 regulatesAnimal cells and systems · 2025Article
- Role of Aspartate 42 and Histidine 79 in the aiPLA2 activity and oligomeric status of Prdx6 at low pH.Research square · 2024Article
- Peroxiredoxin 6 suppresses ferroptosis in lung endothelial cells.Free radical biology & medicine · 2024Article
- The Role of Phospholipase Activity of Peroxiredoxin 6 in Its Transmembrane Transport and Protective Properties.International journal of molecular sciences · 2022Article
- An infection-induced oxidation site regulates legumain processing and tumor growth.Nature chemical biology · 2022Article
- Basis for using thioredoxin as an electron donor by Schizosaccharomyces pombe Gpx1 and Tpx1.AMB Express · 2022Article
- Superoxide Radicals in the Execution of Cell Death.Antioxidants (Basel, Switzerland) · 2022Review
- Peroxiredoxin 6 Peroxidase and CaAntioxidants (Basel, Switzerland) · 2022Article
- Wittig reagents for chemoselective sulfenic acid ligation enables global site stoichiometry analysis and redox-controlled mitochondrial targeting.Nature chemistry · 2021Article
- Identification of peroxiredoxin 6 as a direct target of withangulatin A by quantitative chemical proteomics in non-small cell lung cancer.Redox biology · 2021Article
- Peroxiredoxins-The Underrated Actors during Virus-Induced Oxidative Stress.Antioxidants (Basel, Switzerland) · 2021Review
- Regulation of Prdx6 by Nrf2 Mediated Through aiPLA2 in White Matter Reperfusion Injury.Molecular neurobiology · 2021Article
- Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation.Molecules (Basel, Switzerland) · 2021Review
- Structural basis of peroxidase catalytic cycle of human Prdx6.Scientific reports · 2020Article
- Non-redox cycling mechanisms of oxidative stress induced by PM metals.Free radical biology & medicine · 2020Review
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Peroxiredoxin 6 (Prdx6) is a unique 1-Cys member of the peroxiredoxin family with both GSH peroxidase and phospholipase A2 (PLA2) activities. It is highly expressed in the lung where it plays an important role in antioxidant defense and lung surfactant metabolism. Glutathionylation of Prdx6 mediated by its heterodimerization with GSH S-transferase π (πGST) is required for its peroxidatic catalytic cycle. Recombinant human Prdx6 crystallizes as a homodimer and sedimentation equilibrium analysis confirmed that this protein exists as a high affinity dimer in solution. Based on measurement of molecular mass, dimeric Prdx6 that was oxidized to the sulfenic acid formed a sulfenylamide during storage. After examination of the dimer interface in the crystal structure, we postulated that the hydrophobic amino acids L145 and L148 play an important role in homodimerization of Prdx6 as well as in its heterodimerization with πGST. Oxidation of Prdx6 also was required for its heterodimerization. Sedimentation equilibrium analysis and the Duolink proximity ligation assay following mutation of the L145 and L148 residues of Prdx6 to Glu indicated greatly decreased dimerization propensity reflecting the loss of hydrophobic interactions between the protein monomers. Peroxidase activity was markedly reduced by mutation at either of the Leu sites and was essentially abolished by the double mutation, while PLA2 activity was unaffected. Decreased peroxidase activity following mutation of the interfacial leucines presumably is mediated via impaired heterodimerization of Prdx6 with πGST that is required for reduction and re-activation of the oxidized enzyme.
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