{
  "abstract": "Ena/VASP proteins are powerful actin polymerases that accumulate at sites of active actin assembly, including lamellipodial and microspike tips, focal adhesions and pathogen surfaces, where they drive processive filament elongation. However, the mechanisms controlling their recruitment remain elusive. Here, we used cells lacking all Ena/VASP-family members to systematically test phosphomimetic and nonphosphorylatable substitutions at conserved tyrosine and serine residues implicated in subcellular targeting. Combining cell-based reconstitution with biochemical assays, we identify phosphorylation of Y16 in vertebrate Ena/VASP proteins as the decisive inhibitory modification controlling subcellular Ena/VASP recruitment, in contrast to previously proposed roles for Y39 and S157. Corresponding phosphomimetic substitutions in the C. elegans orthologue UNC-34 phenocopied uncoordinated locomotion of UNC-34 null worms, supporting the evolutionary conservation of this regulatory mechanism. Thus, our findings identify a conserved phosphorylation-sensitive switch at the EVH1-FP4 ligand interface that links EVH1-dependent targeting to dynamic control of actin assembly in adhesion, migration and pathogenesis.",
  "abstract_shown": true,
  "affiliations": [
    "Institute for Biophysical Chemistry, Hannover Medical School, Carl-Neuberg-Strasse 1, 30625 Hannover, Germany",
    "Molecular Cell Biology Group, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124 Braunschweig, Germany",
    "Division of Molecular Cell Biology, Institute for Cell and Neurobiology, Technische Universität Braunschweig, Spielmannstraße 7, 38106 Braunschweig, Germany",
    "Gray School of Medical Sciences, Gray Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv, Israel",
    "Braunschweig Integrated Centre of Systems Biology (BRICS), Rebenring 56, 38106 Braunschweig, Germany"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 10,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Jonas Scholz",
      "orcid": "0009-0000-4789-4249"
    },
    {
      "affs": [
        1,
        2
      ],
      "name": "Julian Kaltenhäuser",
      "orcid": "0009-0002-7780-4771"
    },
    {
      "affs": [
        3
      ],
      "name": "Jerushah Emerald"
    },
    {
      "affs": [
        0
      ],
      "name": "Pavel Kats",
      "orcid": "0009-0003-0908-6621"
    },
    {
      "affs": [
        0
      ],
      "name": "Thomas Kaufmann",
      "orcid": "0009-0003-5907-299X"
    },
    {
      "affs": [
        3
      ],
      "name": "Anat Nitzan",
      "orcid": "0009-0007-0756-7500"
    },
    {
      "affs": [
        0
      ],
      "name": "Ute Curth"
    },
    {
      "affs": [
        1,
        2,
        4
      ],
      "name": "Klemens Rottner",
      "orcid": "0000-0003-4244-4198"
    },
    {
      "affs": [
        3
      ],
      "name": "Ronen Zaidel-Bar",
      "orcid": "0000-0002-1374-5007"
    },
    {
      "affs": [
        0
      ],
      "name": "Jan Faix",
      "orcid": "0000-0003-1803-9192"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/8b64kgzk3mq1y.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.26.761804",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.26.761804v1.full",
  "id": "8b64kgzk3mq1y",
  "issns": [
    "2692-8205"
  ],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.26.761804v1",
  "language": "en",
  "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"
    ],
    [
      "heading",
      "Article"
    ],
    [
      "openalex",
      "1307|Cellular Mechanics and Interactions"
    ]
  ],
  "openalex": "W7224092260",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.26.761804v1.full.pdf",
  "pmcid": "PMC13733861",
  "pmid": "42990243",
  "published": "2026-10-26",
  "publisher": "Cold Spring Harbor Laboratory Preprints",
  "ris": "https://research.draconitic.com/paper/8b64kgzk3mq1y.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:29:59Z",
      "native_id": "10.64898/2026.10.26.761804",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.26.761804v1"
    },
    {
      "first_seen": "2026-11-08T12:23:33Z",
      "native_id": "PMC13733861",
      "source": "pmc",
      "url": "https://doi.org/10.64898/2026.10.26.761804"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "biorxiv:cell biology",
      "subfield": "cell-biology"
    }
  ],
  "title": "Conserved tyrosine Y16 acts as a phosphorylation switch controlling Ena/VASP recruitment to sites of actin assembly",
  "title_text": "Conserved tyrosine Y16 acts as a phosphorylation switch controlling Ena/VASP recruitment to sites of actin assembly",
  "type": "preprint",
  "updated_at": "2026-11-08T12:23:33Z",
  "url": "https://research.draconitic.com/paper/8b64kgzk3mq1y",
  "venue": "bioRxiv",
  "versions": []
}