{
  "abstract": "SUMMARY Eukaryotic cells contain multiple biochemically distinct actin filament networks, which enable versatile functions of actin in a range of cellular processes. Yet, the mechanisms by which specific actin filament networks are assembled in a common cytoplasm remain elusive. Here, we investigated how functionally distinct actin nanoscale layers, specified by α-actinin and tropomyosin isoforms, Tpm1.6 and Tpm3.2, are assembled at focal adhesions. By combining genetic perturbations with mitochondrial-targeting of actin polymerases, we discovered that DAAM1 formin assembles Tpm3.2-actin filaments, whereas Ena/VASP family proteins polymerize α-actinin cross-linked actin filament bundles at focal adhesions. Consequently, loss of DAAM1 dampened Tpm3.2 protein levels and impaired focal adhesion disassembly, thus phenocopying Tpm3.2-deficient cells. In contrast, Ena/VASP depletion led to defective focal adhesion maturation and loss of α-actinin from focal adhesions. More broadly, our study highlights specific roles for formin and Ena/VASP family proteins in assembling biochemically and functionally distinct linear actin filament arrays in cells.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "name": "Xiang Le Chua"
    },
    {
      "name": "Parijat Biswas"
    },
    {
      "name": "Hugo Wioland"
    },
    {
      "name": "Pekka Lappalainen"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/dj7npm6fh03gc.bib",
  "cited_by": 1,
  "doi": "10.64898/2026.08.19.745742",
  "fulltext_url": null,
  "id": "dj7npm6fh03gc",
  "issns": [],
  "landing_url": "https://hal.science/hal-05770766v1",
  "language": "en",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "hal",
      "1.sdv.bc"
    ],
    [
      "hal",
      "2.sdv.bc.bc"
    ],
    [
      "openalex",
      "1307|Cellular Mechanics and Interactions"
    ]
  ],
  "openalex": "W7203824822",
  "pdf_url": "https://hal.science/hal-05770766/document",
  "pmcid": null,
  "pmid": null,
  "published": "2026-08-20",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/dj7npm6fh03gc.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:43Z",
      "native_id": "hal-05770766",
      "source": "hal",
      "url": "https://hal.science/hal-05770766v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "hal:1.sdv.bc",
      "subfield": "cell-biology"
    }
  ],
  "title": "DAAM1 formin and Ena/VASP proteins assemble functionally distinct actin filaments for focal adhesions",
  "title_text": "DAAM1 formin and Ena/VASP proteins assemble functionally distinct actin filaments for focal adhesions",
  "type": "preprint",
  "updated_at": "2026-10-30T12:17:43Z",
  "url": "https://research.draconitic.com/paper/dj7npm6fh03gc",
  "venue": "HAL",
  "versions": []
}