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Molecular and Cellular Biology, October 2003, p. 7291-7304, Vol. 23, No. 20
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.20.7291-7304.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Distinct Rho GTPase Activities Regulate Epithelial Cell Localization of the Adhesion Molecule CEACAM1: Involvement of the CEACAM1 Transmembrane Domain

Bénédicte Fournès,1 Jennifer Farrah,1,2 Melanie Olson,1 Nathalie Lamarche-Vane,3 and Nicole Beauchemin1,2,4*

McGill Cancer Centre,1 Department of Biochemistry,2 Department of Anatomy and Cell Biology,3 Departments of Medicine and Oncology, McGill University, Montreal, Quebec, Canada4

Received 29 April 2003/ Returned for modification 4 June 2003/ Accepted 15 July 2003

CEACAM1 is an intercellular adhesion glycoprotein. As CEACAM1 plays an important role in epithelial cell signaling and functions, we have examined its localization in epithelial cells. We have observed that distribution at cell contacts is not always seen in these cells, suggesting that CEACAM1 localization might be regulated. In Swiss 3T3 cells, the targeting of CEACAM1 at cell-cell boundaries is regulated by the Rho GTPases. In the present study, we have used the MDCK epithelial cells to characterize the effects of the Rho GTPases and their effectors on CEACAM1 intercellular targeting. Activated Cdc42 and Rac1 or their downstream effector PAK1 targeted CEACAM1 to sites of cell-cell contacts. On the other hand, neither activated RhoA nor activated Rho kinase directed CEACAM1 to cell boundaries, resulting in a condensed distribution of CEACAM1 at the cell surface. Interestingly, inhibition of this pathway resulted in CEACAM1 intercellular localization suggesting that a tightly regulated balance of Rho GTPase activities is necessary to target CEACAM1 at cell-cell boundaries. In addition, using CEACAM1 mutants and chimeric fusion constructs containing domains of the colony-stimulating factor receptor, we have shown that the transmembrane domain of CEACAM1 is responsible for the Cdc42-induced targeting at cell-cell contacts.

* Corresponding author. Mailing address: McGill Cancer Centre, McGill University, 3655 Promenade Sir-William-Osler, Room 711, Montreal, Quebec H3G 1Y6, Canada. Phone: (514) 398-3541. Fax: (514) 398-6769. E-mail: nicole.beauchemin{at}mcgill.ca.

Molecular and Cellular Biology, October 2003, p. 7291-7304, Vol. 23, No. 20
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.20.7291-7304.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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