Abstract
The coxsackie and adenovirus receptor (CAR) is a transmembrane receptor that plays a key role in controlling adhesion between adjacent epithelial cells. CAR is highly expressed in epithelial cells and was originally identified as a primary receptor for adenovirus cell binding. However, studies over the last 10 years have demonstrated that CAR plays a key role in co-ordinating cell–cell adhesion under homeostatic conditions including neuronal and cardiac development and cell junction stability; it has also been implicated in pathological states such as cancer growth and leukocyte transmigration during inflammation. Here we provide an overview of the functions of CAR as an adhesion molecule and highlight the emerging important role for CAR in controlling both recruitment of immune cells and in tumorigenesis.
Highlights
The Coxsackie and adenovirus receptor CXADR or coxsackie and adenovirus receptor (CAR), known as CAR-like membrane protein (CLMP) was first identified as a highaffinity receptor for the coxsackie B virus and adenovirus (Ad) serotypes 2 and 5 (Bergelson et al, 1997) and was subsequently shown to belong to the Junction Adhesion Molecule (JAM) family within the immunoglobulin (Ig) superfamily (IgSF) of proteins that localise in tight junctions and along the lateral membrane of epithelial cells (Coyne and Bergelson, 2005)
Studies over the last 10 years have demonstrated that CAR plays a key role in co-ordinating cell–cell adhesion under homeostatic conditions including neuronal and cardiac development and cell junction stability; it has been implicated in pathological states such as cancer growth and leukocyte transmigration during inflammation
The Coxsackie and adenovirus receptor CXADR or CAR, known as CAR-like membrane protein (CLMP) was first identified as a highaffinity receptor for the coxsackie B virus and adenovirus (Ad) serotypes 2 and 5 (Bergelson et al, 1997) and was subsequently shown to belong to the Junction Adhesion Molecule (JAM) family within the immunoglobulin (Ig) superfamily (IgSF) of proteins that localise in tight junctions and along the lateral membrane of epithelial cells (Coyne and Bergelson, 2005)
Summary
The Coxsackie and adenovirus receptor CXADR or CAR, known as CAR-like membrane protein (CLMP) was first identified as a highaffinity receptor for the coxsackie B virus and adenovirus (Ad) serotypes 2 and 5 (Bergelson et al, 1997) and was subsequently shown to belong to the Junction Adhesion Molecule (JAM) family within the immunoglobulin (Ig) superfamily (IgSF) of proteins that localise in tight junctions and along the lateral membrane of epithelial cells (Coyne and Bergelson, 2005). JAM proteins are found in intercellular junctions of endothelial cells and on the surface of leukocytes, platelets and eyrthrocytes (Luissint et al, 2014). JAM proteins have been implicated in a diverse array of functions involving cell–cell adhesion including barrier function, leukocyte migration, platelet activation angiogenesis and reovirus binding (Garrido-Urbani et al, 2014). JAMs are type I transmembrane glycoproteins, composed of two extracellular Ig-like domains, one transmembrane domain and one cytoplasmic tail of variable length containing a PDZ domain. CAR, Endothelial Selective Adhesion Molecule (ESAM), JAM-L and JAM-4 make up a separate subfamily and have longer cytoplasmic tails. JAMs associate with adaptor/signalling proteins through the PDZ domain in the C-terminus and homo or hetero-dimerize with other JAMs via the extracellular domain (Garrido-Urbani et al, 2014)
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
