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Originally published In Press as doi:10.1074/jbc.M105077200 on August 15, 2001

J. Biol. Chem., Vol. 276, Issue 42, 39282-39289, October 19, 2001
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CD98-mediated Links between Amino Acid Transport and beta 1 Integrin Distribution in Polarized Columnar Epithelia*

Didier MerlinDagger , Shanthi Sitaraman, Xia Liu, Karen Eastburn, Jun Sun, Torsten Kucharzik, Brian Lewis, and James L. Madara

From the Epithelial Pathology Unit, Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, Georgia 30322

In non-polarized cells, CD98 has been shown to both influence beta 1 integrins and heterodimerize with LAT-2, which confers amino acid transport capability on the LAT-2/CD98 heterodimer. Since LAT-2 is most heavily expressed in intestine and CD98 associates with the beta 1 integrin splice form selectively found in such epithelia, we investigated the relationship and polarity of these proteins using the intestinal epithelial model Caco2-BBE. CD98 was found to selectively coimmunoprecipitate with both LAT-2 and beta 1 integrin, and, logically, all three proteins were polarized to the same (basolateral) domain. Furthermore, expression of CD98 in polarized epithelia lacking human CD98 (MDCK cells) disrupted beta 1 integrin surface distribution and cytoskeletal architecture, suggesting that CD98 can influence integrin function. Expression of a CD98 mutant lacking the specific residues conferring LAT-2 binding similarly affected cells, confirming that the latter effect was not due to LAT-2 sequestration. Use of CD98 truncation mutants suggest that a 10-amino acid domain located at the putative cytoplasmic tail/transmembrane domain interface was necessary and sufficient to induce the phenotype change. We conclude that the CD98/LAT-2 amino acid transporter is polarized to the same domain on which beta 1 integrin resides. CD98 appears to associate with beta 1 integrin and, in doing so, may influence its function as revealed by disruption of the outside-in signaling that confers cytoskeletal organization. Furthermore, such findings suggest a link between classic transport events and a critical element of barrier function: integrin-mediated influences on cytoskeletal organization.

* This work was supported by National Institutes of Health Grants DK-02831 (to D. M.), DK-02802 (to S. S.), and DK-47662 and DK-35932 (both to J. L. M.). This work was initiated with a career development award from the Crohn's and Colitis Foundation of America (to D. M. and S. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Recipient of a 2001 Young Investigator award from the Crohn's and Colitis Foundation of America. To whom correspondence should be addressed: Dept. of Pathology and Laboratory Medicine, Emory University, 1639 Pierce Dr., Atlanta, GA 30322. Tel.: 404-712-7726; Fax: 419-821-3041; E-mail: dmerlin@emory.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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