Abstract
The coxsackievirus and adenovirus receptor (CAR, CXADR) is a multi-functional cell adhesion molecule which forms with CLMP, BT-IgSF, ESAM and CTX a structural subgroup within the Ig superfamily. These proteins share an overall domain organization with two extracellular Ig domains, a transmembrane region and a cytoplasmic tail which includes a PDZ binding motif. CAR is strongly expressed in brain and heart during embryonic development and becomes down-regulated in early postnatal stages. Cell adhesion experiments, binding studies and as well as crystallographic investigations on the extracellular domain reveal a flexible ectodomain for CAR that mediates homophilic and heterophilic binding. Several animal models showed an essential role for CAR during embryonic heart development and for electrical conduction between neighboring cardiomyocytes at mature stages. CAR gets re-expressed in diseased or damaged cardiac tissue, probably to induce regeneration and remodeling of the cardiac muscle.
Highlights
The coxsackievirus and adenovirus receptor (CAR, CXADR) is a multi-functional cell adhesion molecule which forms with CLMP, BT-IgSF, ESAM and CTX a structural subgroup within the Ig superfamily
These proteins are composed of two extracellular Ig domains, a short transmembrane region and a cytoplasmic tail (Figure 1A)
By adhesion and binding assays [13,14,15,16] and further by crystallographic studies (Figure 1B,C) using recombinantly expressed human or mouse CAR it was shown that CAR promotes homophilic binding between neighboring cells which is mediated by
Summary
The coxsackie and adenovirus receptor (CAR, CXADR) was initially identified in human and mouse as a common receptor for coxsackie B viruses and adenoviruses of the groups A, C, D, E and F and has been recognized for its involvement in virus-mediated myocarditis [1,2,3,4,5] It is a 46 kD type I transmembrane protein which functions as homophilic and heterophilic cell adhesion protein. CTX (marker for cortical thymocytes of Xenopus) [11,12] These proteins are composed of two extracellular Ig domains, a short transmembrane region and a cytoplasmic tail (Figure 1A). The cytoplasmic tail is generated by alternative splicing variants (CAR1/CAR2) of exon 7 and 8 [32]
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