Seminal studies performed in laboratory of Barry Honig, in particular, showed that cell-cell adhesion receptor, classic cadherin, forms clusters driven by both extracellular and intracellular binding events. This process is essential to reinforce weak trans-interaction of individual cadherin molecules. Recent and ongoing studies show additional functions of cadherin clustering machinery. Continuous and fast reassembly of cadherin clusters within cell-cell contacts makes the contacts highly adhesive and flexible at the same time. Furthermore, the structural compatibility between cis interactions of cadherin molecules in a cluster across its trans interface makes cadherin clustering an ideal sorting mechanism that arranges proteins involved in cadherin-cadherin cis alignment into specialized clusters that are equivalent in structure and number to those in neighboring cells. This feature of cadherin-based adhesion might synchronize signaling events in individual cells in a tissue. This function of cadherin clusters is discussed on the example of two cadherin associated proteins, vinculin and erbin, involved in mechanosensing and growth regulation, correspondingly.

Cluster of cadherin molecules is a universal device for adhesion and signaling

ACS Spring 2022

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