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M302777200v1
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Papers In Press, published online ahead of print April 25, 2003
J. Biol. Chem, 10.1074/jbc.M302777200
Submitted on March 18, 2003
Revised on April 25, 2003
Accepted on April 25, 2003

CD98 and ICAM-1 regulate the activity of amino acid transporter LAT-2 in polarized intestinal epithelia

Xia Liu, Laetitia Charrier, Andrew Gewirtz, Shanthi Sitaraman, and Didier Merlin

Medicine Dept., Emory University, Atlanta, GA 30322

Corresponding Author: dmerlin{at}emory.edu

We have previously shown that the heterodimer CD98/LAT-2 (LAT-2: amino acid transporter) is expressed in the basolateral membrane intestinal of epithelial cells and is associated with ƒÒ1 integrin (J. Biol. Chem. 39282-39289, 2001). In the present study we examined the interaction of CD98/LAT2 with ICAM-1 and the potential of such interaction on the activation of intracellular signal in Caco2-BBE cell monolayers. ICAM-1 was found to be expressed to the basolateral domain and selectively coimmunoprecipitate with CD98/LAT-2 in Caco2-BBE monolayers. Using antibodies as ligands to CD98 and ICAM-1, we demonstrate that the basolateral cross-linking of CD98 and ICAM-1 differentially affect the intrinsic activity of the LAT-2 transporter. While CD98 ligation decreases the Km and Vm of the LAT-2 transporter, ICAM-1 ligation increases Km and Vm of the amino acid transporter LAT-2. In addition, basolateral cross-linking of CD98 or ICAM-1 induces threonine phosphorylation of a ~ 160 kDa supra molecular complex that is consistent with CD98/LAT-2 ¡VICAM-1 complex. Together these findings demonstrate that i) CD98/LAT-2 interacts with ICAM-1 in Caco2-BBE cell monolayers ii) CD98 and ICAM-1 ligands generate intracellular signals that regulate the amino acids transporter (LAT-2) activity. Our data provide a novel mechanism by which events such as adhesion may be integrated by amino acid transport activity resulting from the direct interaction of cell surface molecules such as CD98 and ICAM-1


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