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Canonical and non-canonical integrin-based adhesions dynamically interconvert

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Item Type:Article
Title:Canonical and non-canonical integrin-based adhesions dynamically interconvert
Creators Name:Lukas, F. and Matthaeus, C. and López-Hernández, T. and Lahmann, I. and Schultz, N. and Lehmann, M. and Puchkov, D. and Pielage, J. and Haucke, V. and Maritzen, T.
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.
Keywords:Cytoskeleton, Focal Adhesion, Integrin Signalling, Integrins
Source:Nature Communications
Publisher:Nature Publishing Group
Page Range:2093
Date:7 March 2024
Official Publication:https://doi.org/10.1038/s41467-024-46381-x
PubMed:View item in PubMed

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