Intestinal epithelial CD98: an oligomeric and multifunctional protein.
The intestinal epithelial cell-surface molecule, CD98 is a type II membrane glycoprotein. Molecular orientation studies have demonstrated that the C-terminal tail of human CD98 (hCD98), which contains a PDZ-binding domain, is extracellular. In intestinal epithelial cells, CD98 is covalently linked to an amino-acid transporter with which it forms a heterodimer. This heterodimer associates with beta(1)-integrin and intercellular adhesion molecular 1 (ICAM-1) to form a macromolecular complex in the basolateral membranes of polarized intestinal epithelial cells. This review focuses on the multifunctional roles of CD98, including involvement in extracellular signaling, adhesion/polarity, and amino-acid transporter expression in intestinal epithelia. A role for CD98 in intestinal inflammation, such as Intestinal Bowel Disease (IBD), is also proposed.
Yan
Yutao
Y
Department of Medicine, Division of Digestive Diseases, Emory University School of Medicine, 615 Michael Street, Atlanta, GA 30322, USA.
Vasudevan
Sona
S
Nguyen
Hang Thi Thu
HT
Merlin
Didier
D
D026905:Amino Acid Transport Systems / Q000378:metabolism; D000818:Animals; D002448:Cell Adhesion; D016764:Cell Polarity; D027261:Fusion Regulatory Protein-1 / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D007413:Intestinal Mucosa / Q000378:metabolism* / Q000473:pathology; D020836:Protein Structure, Quaternary
D026905:Amino Acid Transport Systems; D027261:Fusion Regulatory Protein-1