The coxsackie virus and adenovirus receptor (CXADR, CAR) is a highly conserved, single-transmembrane glycoprotein and the primary receptor to mediate cellular attachment and infection of coxsackie B viruses and most adenoviruses. The CAR protein contains a pair of Ig-like domains within the amino-terminal extracellular domain and a carboxyl-terminal PDZ motif. Research studies indicate that CAR is a tight junction protein that associates with the ZO-1 scaffold protein and promotes both cell adhesion and restriction of solute and ion movement between cells. Endogenous CAR is targeted to the basolateral plasma membrane by a tyrosine-based basolateral sorting signal and clathrin adaptors AP-1A and AP-1B. CAR binds junctional adhesion molecule L (JAML) on epithelial cells and neutrophils where it activates PI3K and downstream MAPK kinases to stimulate epithelial γδ T cell proliferation and increase production of TNFα and keratinocyte growth factor. As a result, the CAR protein plays a potentially critical role in adenoviral gene therapy, immunity, wound repair, inflammation, and cancer therapy. Additional studies demonstrate that CAR is essential in regulating squamous carcinoma cell growth.

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