{"entity": "publication", "iuid": "c3f74b41f9be44d2ba332d6d5c86782a", "timestamp": "2026-07-22T22:20:23.244Z", "links": {"self": {"href": "https://publications.scilifelab.se/publication/c3f74b41f9be44d2ba332d6d5c86782a.json"}, "display": {"href": "https://publications.scilifelab.se/publication/c3f74b41f9be44d2ba332d6d5c86782a"}}, "title": "Copper ionophore elicits calpain-dependent paraptosis coincident with proteotoxic stress.", "authors": [{"family": "Sae-Fung", "given": "Apiwit", "initials": "A"}, {"family": "Fadeel", "given": "Bengt", "initials": "B"}], "type": "journal article", "published": "2025-12-12", "journal": {"title": "Cell Commun Signal", "issn": "1478-811X", "volume": "24", "issue": "1", "pages": "47", "issn-l": null}, "abstract": "Copper is essential to all living organisms. However, too much copper is deleterious, and cellular copper content is therefore subject to tight control. Excess copper was recently found to perturb a set of metabolic enzymes in mitochondria, leading to the aggregation of these proteins and the demise of the cell. However, our understanding of the mechanism of copper-dependent cell death remains incomplete. Here, we report that copper ionophore (elesclomol)-induced cell death is calpain-dependent, featuring dilation of the endoplasmic reticulum along with perinuclear clustering of mitochondria. Moreover, elesclomol evoked proteotoxic stress, manifested as a disruption of ubiquitin and proteasome homeostasis, coupled with a conserved heat shock response. Overall, these results have shown that elesclomol promotes calpain-dependent paraptosis with the involvement of both mitochondrial and extramitochondrial compartments of the cell.", "doi": "10.1186/s12964-025-02558-5", "pmid": "41388416", "labels": {"Chemical Proteomics": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC12837948"}, {"db": "pii", "key": "10.1186/s12964-025-02558-5"}], "notes": [], "created": "2026-01-31T17:47:09.857Z", "modified": "2026-01-31T17:47:09.861Z"}