Focal adhesions, reticular adhesions, flat clathrin lattices: what divides them, what unites them?

The majority of cells within multicellular organisms requires anchorage to their surroundings in the form of cell-cell or cell-matrix adhesions. In regards to cell-matrix adhesions, the transmembrane receptors of the integrin family have long been recognized as the central scaffold around which these adhesion complexes are built. Via their extracellular domains integrins bind extracellular matrix ligands while their intracellular tails interact with a plethora of proteins that link integrin-based adhesions to the cytoskeleton and turn them also into important signaling platforms. Depending on the specific intracellular interactome of the integrins, different types of integrin adhesion complexes have been classified. The best-studied ones are the focal adhesions, in which integrins become firmly linked to contractile actomyosin fibers, allowing force transduction. But integrins also form an integral part of adhesion structures that lack the strong actomyosin link and are enriched in endocytic proteins. These have been named reticular adhesions, flat clathrin lattices, or clathrin plaques. Initially, the different types of integrin adhesion complexes have been viewed as discrete entities with their own separate life cycles. However, in the past years it has become more and more apparent how closely intertwined they are. In fact, it was shown that they can trigger each other's biogenesis or can even directly convert into each other. Here, we describe similarities as well as differences between integrin adhesion complexes, focusing on the versatile αvβ5 integrins, and discuss the recently discovered close links and interconversion modes between the different αvβ5 integrin adhesion types.