ArticleAntioxidants & redox signaling2015
When an Intramolecular Disulfide Bridge Governs the Interaction of DUOX2 with Its Partner DUOXA2.
Article in Antioxidants & redox signaling, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- Functional Domain Mapping of TPO: Insights From 6 Variants in Sudanese Kindreds With Congenital Hypothyroidism.The Journal of clinical endocrinology and metabolism · 2026Article
- NADPH oxidases: redox regulation of cell homeostasis and disease.Physiological reviews · 2025Review
- DUOX1 in mammalian disease pathophysiology.Journal of molecular medicine (Berlin, Germany) · 2021Review
- Exercise-Stimulated ROS Sensitive Signaling Pathways in Skeletal Muscle.Antioxidants (Basel, Switzerland) · 2021Review
- Oxidants in Physiological Processes.Handbook of experimental pharmacology · 2021Review
- Structures of mouse DUOX1-DUOXA1 provide mechanistic insights into enzyme activation and regulation.Nature structural & molecular biology · 2020Article
- The role of dual oxidases in physiology and cancer.Genetics and molecular biology · 2020Article
- HAntioxidants (Basel, Switzerland) · 2019Review
- Antimicrobial actions of dual oxidases and lactoperoxidase.Journal of microbiology (Seoul, Korea) · 2018Review
- Dual oxidase: a novel therapeutic target in allergic disease.British journal of pharmacology · 2018Review
- HIV-1 Tat protein induces DNA damage in human peripheral blood B-lymphocytes via mitochondrial ROS production.Redox biology · 2018Article
- Paradoxical roles of dual oxidases in cancer biology.Free radical biology & medicine · 2017Review
- Acrolein and thiol-reactive electrophiles suppress allergen-induced innate airway epithelial responses by inhibition of DUOX1 and EGFR.American journal of physiology. Lung cellular and molecular physiology · 2016Article
- Genetic disorders coupled to ROS deficiency.Redox biology · 2015Review
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Authors and funding
10 authors at 5 institutions in 4 countries.
Funding
Abstract
aimsThe dual oxidase 2 (DUOX2) protein belongs to the NADPH oxidase (NOX) family. As H2O2 generator, it plays a key role in both thyroid hormone biosynthesis and innate immunity. DUOX2 forms with its maturation factor, DUOX activator 2 (DUOXA2), a stable complex at the cell surface that is crucial for the H2O2-generating activity, but the nature of their interaction is unknown. The contribution of some cysteine residues located in the N-terminal ectodomain of DUOX2 in a surface protein-protein interaction is suggested. We have investigated the involvement of different cysteine residues in the formation of covalent bonds that could be of critical importance for the function of the complex.
resultsWe report the identification and the characterization of an intramolecular disulfide bond between cys-124 of the N-terminal ectodomain and cys-1162 of an extracellular loop of DUOX2, which has important functional implications in both export and activity of DUOX2. This intramolecular bridge provides structural support for the formation of interdisulfide bridges between the N-terminal domain of DUOX2 and the two extracellular loops of its partner, DUOXA2. INNOVATION: Both stability and function of the maturation factor, DUOXA2, are dependent on the oxidative folding of DUOX2, indicating that DUOX2 displays a chaperone-like function with respect to its partner.
conclusionsThe oxidative folding of DUOX2 that takes place in the endoplasmic reticulum (ER) appears to be a key event in the trafficking of the DUOX2/DUOXA2 complex as it promotes an appropriate conformation of the N-terminal region, which is propitious to subsequent covalent interactions with the maturation factor, DUOXA2.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.