{
  "abstract": "Mitochondrial cristae disintegration is a hallmark of heart failure, yet how oxidative phosphorylation (OXPHOS) dysfunction triggers this structural collapse remains unclear. Here we identify acetylation of the complex I subunit NDUFA13 at lysine 7 (K7) as a metabolic sensor coupling OXPHOS dysfunction to cristae remodelling. OXPHOS inhibition drove NDUFA13-K7 hyperacetylation, inducing conformational compaction and translocation to the intermembrane space. Acetylated NDUFA13 competitively engaged PHB2 through its coiled-coil domain, displacing PHB1 and disassembling prohibitin scaffolds. The acetylation-mimetic NDUFA13-K7Q induced cristae fragmentation in vitro, and cardiomyocyte-specific K7Q knock-in mice showed accelerated mortality and cristae loss under pressure overload, accompanied by impaired TCA cycle flux, defective fatty acid oxidation and selective depletion of polyunsaturated cardiolipins. These findings establish NDUFA13-K7 acetylation as a reversible switch converting bioenergetic failure into pathological cristae remodelling and metabolic reprogramming, highlighting therapeutic potential for targeted deacetylation.",
  "abstract_shown": true,
  "affiliations": [
    "School of Medicine, Zhejiang University"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 22,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "J. Nan"
    },
    {
      "name": "X. Yang"
    },
    {
      "name": "Y. Lin"
    },
    {
      "name": "J. Shen"
    },
    {
      "name": "H. Chen"
    },
    {
      "name": "Z. Xu"
    },
    {
      "name": "J. Ye"
    },
    {
      "name": "Y. Wang"
    },
    {
      "name": "D. Xiong"
    },
    {
      "name": "C. Ke"
    },
    {
      "name": "L. Zhu"
    },
    {
      "name": "X. Kong"
    },
    {
      "name": "Z. Zhong"
    },
    {
      "name": "T. Ren"
    },
    {
      "name": "J. Jiang"
    },
    {
      "name": "X. Wang"
    },
    {
      "name": "B. Wang"
    },
    {
      "name": "D. Zhao"
    },
    {
      "name": "Z.-z. Li"
    },
    {
      "name": "Z. Shao"
    },
    {
      "name": "B. Liu"
    },
    {
      "name": "X. He"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/f5tmzpft72cs2.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.26.761921",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.26.761921v1.full",
  "id": "f5tmzpft72cs2",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.26.761921v1",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "cell biology"
    ],
    [
      "openalex",
      "1312|Mitochondrial Function and Pathology"
    ]
  ],
  "openalex": "W7224134538",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.26.761921v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-26",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/f5tmzpft72cs2.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:30:05Z",
      "native_id": "10.64898/2026.10.26.761921",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.26.761921v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "biorxiv:cell biology",
      "subfield": "cell-biology"
    }
  ],
  "title": "Acetylation of NDUFA13 at K7 Senses OXPHOS Dysfunction to Disrupt Prohibitin Scaffolds and Drive Cristae Remodelling in Heart Failure",
  "title_text": "Acetylation of NDUFA13 at K7 Senses OXPHOS Dysfunction to Disrupt Prohibitin Scaffolds and Drive Cristae Remodelling in Heart Failure",
  "type": "preprint",
  "updated_at": "2026-10-30T12:30:05Z",
  "url": "https://research.draconitic.com/paper/f5tmzpft72cs2",
  "venue": "bioRxiv",
  "versions": []
}