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Canonical and non-canonical integrin-based adhesions dynamically interconvert

Author

Listed:
  • Fabian Lukas

    (RPTU Kaiserslautern-Landau
    Leibniz-Forschungsinstitut für Molekulare Pharmakologie)

  • Claudia Matthaeus

    (National Heart, Lung, and Blood Institute, National Institutes of Health
    Leibniz-Forschungsinstitut für Molekulare Pharmakologie)

  • Tania López-Hernández

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie)

  • Ines Lahmann

    (Max-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC))

  • Nicole Schultz

    (RPTU Kaiserslautern-Landau)

  • Martin Lehmann

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie)

  • Dmytro Puchkov

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie)

  • Jan Pielage

    (RPTU Kaiserslautern-Landau)

  • Volker Haucke

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie
    Freie Universität Berlin
    Charité Universitätsmedizin Berlin)

  • Tanja Maritzen

    (RPTU Kaiserslautern-Landau
    Leibniz-Forschungsinstitut für Molekulare Pharmakologie)

Abstract

Adhesions are critical for anchoring cells in their environment, as signaling platforms and for cell migration. In line with these diverse functions different types of cell-matrix adhesions have been described. Best-studied are the canonical integrin-based focal adhesions. In addition, non-canonical integrin adhesions lacking focal adhesion proteins have been discovered. These include reticular adhesions also known as clathrin plaques or flat clathrin lattices, that are enriched in clathrin and other endocytic proteins, as well as extensive adhesion networks and retraction fibers. How these different adhesion types that share a common integrin backbone are related and whether they can interconvert is unknown. Here, we identify the protein stonin1 as a marker for non-canonical αVβ5 integrin-based adhesions and demonstrate by live cell imaging that canonical and non-canonical adhesions can reciprocally interconvert by the selective exchange of components on a stable αVβ5 integrin scaffold. Hence, non-canonical adhesions can serve as points of origin for the generation of canonical focal adhesions.

Suggested Citation

  • Fabian Lukas & Claudia Matthaeus & Tania López-Hernández & Ines Lahmann & Nicole Schultz & Martin Lehmann & Dmytro Puchkov & Jan Pielage & Volker Haucke & Tanja Maritzen, 2024. "Canonical and non-canonical integrin-based adhesions dynamically interconvert," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-46381-x
    DOI: 10.1038/s41467-024-46381-x
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    References listed on IDEAS

    as
    1. Bijeta Prasai & Gideon J. Haber & Marie-Paule Strub & Regina Ahn & John A. Ciemniecki & Kem A. Sochacki & Justin W. Taraska, 2021. "The nanoscale molecular morphology of docked exocytic dense-core vesicles in neuroendocrine cells," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    2. Francesco Baschieri & Stéphane Dayot & Nadia Elkhatib & Nathalie Ly & Anahi Capmany & Kristine Schauer & Timo Betz & Danijela Matic Vignjevic & Renaud Poincloux & Guillaume Montagnac, 2018. "Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
    3. Marco A. Alfonzo-Méndez & Kem A. Sochacki & Marie-Paule Strub & Justin W. Taraska, 2022. "Dual clathrin and integrin signaling systems regulate growth factor receptor activation," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
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    5. Claudia Matthaeus & Kem A. Sochacki & Andrea M. Dickey & Dmytro Puchkov & Volker Haucke & Martin Lehmann & Justin W. Taraska, 2022. "The molecular organization of differentially curved caveolae indicates bendable structural units at the plasma membrane," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
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