Nectin cell adhesion molecule 2 (NECTIN2)

Nectin cell adhesion molecule 2 (NECTIN2), also known as Nectin-2 or CD112, is a single-pass type I membrane glycoprotein belonging to the immunoglobulin superfamily (IgSF)[1][2]. It is involved in calcium-independent cell–cell adhesion by forming both homophilic and heterophilic interactions, particularly in adherens junctions of fibroblasts, epithelial cells, and synaptic junctions of neurons[1][2]. The extracellular domain contains three Ig-like domains, with the N-terminal variable-type Ig-V domain mediating binding specificity[1]. NECTIN2 interacts with cytoplasmic afadin to link adherens junctions to the actin cytoskeleton[1][2]. Originally named for its role as a herpesvirus entry mediator (Herpesvirus entry mediator B), NECTIN2 also interacts with immune receptors such as DNAM-1 (CD226) and TIGIT, mediating immune cell–tumor cell interactions. Altered NECTIN2 expression is implicated in cancer progression, immune evasion, and viral infections[2].

Other names

Nectin-2CD112Herpesvirus entry mediator BHveBPRR2PVRL2PVRR2poliovirus receptor-like 2poliovirus receptor-related 2herpesvirus entry protein B