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Biochim Biophys Acta. 2008 Oct;1780(10):1087-92. doi: 10.1016/j.bbagen.2008.06.007. Epub 2008 Jun 24.

Intestinal epithelial CD98: an oligomeric and multifunctional protein.

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1
Department of Medicine, Division of Digestive Diseases, Emory University School of Medicine, 615 Michael Street, Atlanta, GA 30322, USA.

Abstract

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.

PMID:
18625289
PMCID:
PMC2602860
DOI:
10.1016/j.bbagen.2008.06.007
[Indexed for MEDLINE]
Free PMC Article
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