{
  "abstract": "Integrin 3{beta}1 (ITG3{beta}1) is a member of an integrin subfamily that binds to laminin proteins and promotes attachment of epithelial cells to the basement membrane. ITG3{beta}1 forms a complex with the tetraspanin CD151, and loss-of-function mutations in both ITG3 and CD151 cause epidermolysis bullosa, a severe skin blistering disease resulting from a defect in basement membrane attachment. Here, we report the cryoEM structure of an ITG3{beta}1 complex with CD151 and show that mutation of CD151 at the binding interface disrupts complex formation in cells. Strikingly, CRISPR-mediated knockout of CD151 leads to a variably penetrant ITG3{beta}1 surface export defect that is restored by re-expression of wild-type but not interface-mutated CD151. Together, these studies define the molecular basis for binding of CD151 to ITG3{beta}1, and show that CD151 promotes ITG3{beta}1 surface export, providing a biochemical explanation for the CD151 loss-of-function phenotype in epidermolysis bullosa.",
  "abstract_shown": true,
  "affiliations": [
    "Harvard Medical School"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "name": "L. Litzau"
    },
    {
      "name": "E. Wren"
    },
    {
      "name": "A. C. Kruse"
    },
    {
      "affs": [
        0
      ],
      "name": "S. C. Blacklow"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/3n9fzfzc7dzgw.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.01.748654",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748654v1.full",
  "id": "3n9fzfzc7dzgw",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748654v1",
  "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",
      "biochemistry"
    ],
    [
      "openalex",
      "2723|Cell Adhesion Molecules Research"
    ]
  ],
  "openalex": "W7207691842",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748654v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-01",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/3n9fzfzc7dzgw.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:52Z",
      "native_id": "10.64898/2026.09.01.748654",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748654v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "openalex:2723|Cell Adhesion Molecules Research",
      "subfield": "immunology"
    }
  ],
  "title": "Structural basis for tetraspanin-dependent surface export and adhesive function of integrin α3β1",
  "title_text": "Structural basis for tetraspanin-dependent surface export and adhesive function of integrin α3β1",
  "type": "preprint",
  "updated_at": "2026-10-30T12:18:52Z",
  "url": "https://research.draconitic.com/paper/3n9fzfzc7dzgw",
  "venue": "bioRxiv",
  "versions": []
}