{
  "abstract": "In open mitosis, re-establishing nucleocytoplasmic compartmentalization requires the LEM2-ESCRT machinery to coordinate spindle clearance with sealing of the remaining nuclear envelope pores. The structural basis of this topologically unique and fundamental membrane-remodeling process is poorly understood. Here, we combine biochemical reconstitution, cryo-electron tomography, subtomogram averaging and large-scale molecular dynamics simulations to define the structural mechanism of nuclear membrane sealing. We structurally resolve that LEM2s winged-helix domain (WH) co-polymerizes with the ESCRT-II/III protein CHMP7 to form a membrane-bound scaffold whose geometry is progressively remodeled by downstream ESCRT-III proteins as it transitions from the flat membrane surrounding the pore towards the negatively curved membrane neck. In parallel, LEM2 positions its intrinsically disordered low-complexity domain within the pore, where condensation around spindle microtubules mechanically couples the membrane-ESCRT-LEM2 scaffold to the spindle and narrows the remaining diffusion path, restoring compartmentalization before membrane closure is complete. Remarkably, the LEM2-WH domain alone forms tightly constricted membrane tubes, coating the negatively curved inner surface, revealing an intrinsic membrane-remodeling activity of the receptor itself. Together, our work establishes a structural framework for how receptor-ESCRT co-polymerization, low complexity domain-mediated sealing and receptor-driven membrane remodeling guide nuclear-envelope pores from spindle-containing openings to terminal constriction and fusion.",
  "abstract_shown": true,
  "affiliations": [
    "Max Planck Institute of Molecular Cell Biology and Genetics"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 13,
  "authors": [
    {
      "name": "M. A. Jordan"
    },
    {
      "name": "K. Palacio-Rodriguez"
    },
    {
      "name": "R. Adakkattil"
    },
    {
      "name": "S. Welsch"
    },
    {
      "name": "L. Niese"
    },
    {
      "name": "D. LaJoie"
    },
    {
      "name": "E. von der Weth"
    },
    {
      "name": "A. Alves Melo"
    },
    {
      "name": "L. Redlingshoefer"
    },
    {
      "name": "S. Otsuka"
    },
    {
      "name": "S. Diez"
    },
    {
      "name": "G. Hummer"
    },
    {
      "affs": [
        0
      ],
      "name": "A. Von Appen"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/4844f4n7cw75b.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.01.748678",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748678v1.full",
  "id": "4844f4n7cw75b",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748678v1",
  "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",
      "molecular biology"
    ],
    [
      "openalex",
      "1312|Nuclear Structure and Function"
    ]
  ],
  "openalex": "W7207618747",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748678v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-01",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/4844f4n7cw75b.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:46Z",
      "native_id": "10.64898/2026.09.01.748678",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748678v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:molecular biology",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Structural mechanism of nuclear membrane sealing by LEM2-ESCRT-III",
  "title_text": "Structural mechanism of nuclear membrane sealing by LEM2-ESCRT-III",
  "type": "preprint",
  "updated_at": "2026-10-30T12:18:46Z",
  "url": "https://research.draconitic.com/paper/4844f4n7cw75b",
  "venue": "bioRxiv",
  "versions": []
}