Canonical and non-canonical integrin-based adhesions dynamically interconvert

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.

Crosstalk of growth factor receptors at plasma membrane clathrin-coated sites

“…This is a function separate from its role in generating membrane curvature and transport vesicles for endocytosis ( 38 – 40 ). Cells use clathrin as small adhesion sites during migration and division ( 41 – 43 ). Of note, in muscle cells, clathrin is used to fortify the PM at sites of actin ( 44 ).…”