Canonical and non-canonical integrin-based adhesions dynamically interconvert

Fabian Lukas, Claudia Matthaeus, Tania López-Hernández, Ines Lahmann, Nicole Schultz, Martin Lehmann, Dmytro Puchkov, Jan Pielage, Volker Haucke and Tanja Maritzen ()
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Fabian Lukas: RPTU Kaiserslautern-Landau
Claudia Matthaeus: National Heart, Lung, and Blood Institute, National Institutes of Health
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
Tanja Maritzen: RPTU Kaiserslautern-Landau

Nature Communications, 2024, vol. 15, issue 1, 1-15

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-46381-x

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