Nectin

Nectins and Nectin-like molecules (Necl) are families of cellular adhesion molecules involved in Ca2+-independent cellular adhesion. Nectins and Nectin-like molecules (Necl) are families of cellular adhesion molecules involved in Ca2+-independent cellular adhesion. Nectins are ubiquitously expressed and have adhesive roles in a wide range of tissues such as the adherens junction of epithelia or the chemical synapse of the neuronal tissue. So far four nectins have been identified in humans, namely nectin-1, nectin-2, nectin-3 and nectin-4. These four family members have also been found in most other well studied mammals. Also, five Necls have been identified, these are: Necl-1, Necl-2, Necl-3, Necl-4 and Necl-5. All nectins and all Necls share the same overall structure defined by three extra cellular immunoglobulin domains, a single transmembrane helix and an intracellular domain. For all nectins the intracellular domain can bind a scaffold protein named afadin (the product of the MLLT4 gene). All nectins and Necls can form homo-cis dimers, meaning a dimer of two alike molecules on the same cell membrane. Following the homo-dimer formation they can trans-interact in an either heterophilic or homophilic manner. The network of the nectin and Necl trans-interactions has been characterized. Recent structural reports reveal the physical and chemical determinants of homophilic interactions mediated by N-terminal IgV domains. In general, heterophilic interactions among nectins have higher affinity than their respective homophilic interactions. Nectins and Necls can also recruit cadherins to enhance binding.