ArticleBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2019
Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1.
Article in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 47 citations in OpenAlex.
- Balancing cellular copper levels via the post-translational regulation of copper transport.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Review
- CCS facilitates the progression of ovarian cancer by suppressing ferroptotic cell death via the modulation of p53-mediated expression of SLC7A11 and GPX4.Acta pharmacologica Sinica · 2026Article
- Review
- The pathogenesis of liver fibrosis in Wilson's disease: hepatocyte injury and regulation mediated by copper metabolism dysregulation.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Review
- Innovative cross-intervention: copper ions and metabolic pathways in cancer therapy.Cancer biology & medicine · 2026Review
- Navigating the copper highway: bacterial strategies for cytoplasmic import.Journal of inorganic biochemistry · 2026Review
- Copper-molybdenum interactions in ruminant nutrition and reproductive physiology: mechanistic insights into growth, digestibility, and follicular development.Frontiers in veterinary science · 2026Review
- Human CTR1 Through the Ages: Milestones and Emerging Roles in Disease and Therapy.Biomolecules · 2025Review
- The molecular mechanisms of cuproptosis and its relevance to atherosclerosis.Biomolecules & biomedicine · 2025Review
- Copper in cancer: friend or foe? Metabolism, dysregulation, and therapeutic opportunities.Cancer communications (London, England) · 2025Review
- Recent Development on Copper-Sensor and its Biological Applications: A Review.Journal of fluorescence · 2025Review
- Copper homeostasis and cuproptosis: implications for neurodegenerative diseases.Frontiers in aging neuroscience · 2025Review
- The role of dysregulated copper metabolism in diabetes and its complications: a review.Frontiers in endocrinology · 2025Review
- Mammalian copper homeostasis: physiological roles and molecular mechanisms.Physiological reviews · 2025Review
- Roles of Copper Transport Systems Members in Breast Cancer.Cancer medicine · 2024Review
- Mechanisms of chondrocyte cell death in osteoarthritis: implications for disease progression and treatment.Journal of orthopaedic surgery and research · 2024Review
- The physiological and pathophysiological roles of copper in the nervous system.The European journal of neuroscience · 2024Review
- Deep learning enables the discovery of a novel cuproptosis-inducing molecule for the inhibition of hepatocellular carcinoma.Acta pharmacologica Sinica · 2024Article
- Copper Metabolism and Cuproptosis: Molecular Mechanisms and Therapeutic Perspectives in Neurodegenerative Diseases.Current medical science · 2024Review
- Adaptive evolution of antioxidase-related genes in hypoxia-tolerant mammals.Frontiers in genetics · 2024Review
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Copper-zinc superoxide dismutase (Sod1) is a critical antioxidant enzyme that rids the cell of reactive oxygen through the redox cycling of a catalytic copper ion provided by its copper chaperone (Ccs). Ccs must first acquire this copper ion, directly or indirectly, from the influx copper transporter, Ctr1. The three proteins of this transport pathway ensure careful trafficking of copper ions from cell entry to target delivery, but the intricacies remain undefined. Biochemical examination of each step in the pathway determined that the activation of the target (Sod1) regulates the Ccs·Ctr1 interaction. Ccs stably interacts with the cytosolic C-terminal tail of Ctr1 (Ctr1c) in a copper-dependent manner. This interaction becomes tripartite upon the addition of an engineered immature form of Sod1 creating a stable Cu(I)-Ctr1c·Ccs·Sod1 heterotrimer in solution. This heterotrimer can also be made by the addition of a preformed Sod1·Ccs heterodimer to Cu(I)-Ctr1c, suggestive of multiple routes to the same destination. Only complete Sod1 activation (i.e. active site copper delivery and intra-subunit disulfide bond formation) breaks the Sod1·Ccs·Ctr1c complex. The results provide a new and extended view of the Sod1 activation pathway(s) originating at cellular copper import.
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