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Originally published In Press as doi:10.1074/jbc.M101907200 on April 18, 2001

J. Biol. Chem., Vol. 276, Issue 25, 22565-22572, June 22, 2001
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A Dileucine Motif Targets E-cadherin to the Basolateral Cell Surface in Madin-Darby Canine Kidney and LLC-PK1 Epithelial Cells*

Kevin C. MirandaDagger §, Tatiana KhromykhDagger , Perpetina ChristyDagger , Tam Luan LeDagger §, Cara J. Gottardi, Alpha S. YapDagger ||**, Jennifer L. StowDagger §, and Rohan D. TeasdaleDagger Dagger Dagger

From the Dagger  Institute for Molecular Bioscience, the § Department of Biochemistry, and the || Department of Physiology & Pharmacology, University of Queensland, Brisbane, Queensland 4072, Australia and the  Memorial Sloan-Kettering Cancer Center, New York, New York 10021

E-cadherin is a major adherens junction protein of epithelial cells, with a central role in cell-cell adhesion and cell polarity. Newly synthesized E-cadherin is targeted to the basolateral cell surface. We analyzed targeting information in the cytoplasmic tail of E-cadherin by utilizing chimeras of E-cadherin fused to the ectodomain of the interleukin-2alpha (IL-2alpha ) receptor expressed in Madin-Darby canine kidney and LLC-PK1 epithelial cells. Chimeras containing the full-length or membrane-proximal half of the E-cadherin cytoplasmic tail were correctly targeted to the basolateral domain. Sequence analysis of the membrane-proximal tail region revealed the presence of a highly conserved dileucine motif, which was analyzed as a putative targeting signal by mutagenesis. Elimination of this motif resulted in the loss of Tac/E-cadherin basolateral localization, pinpointing this dileucine signal as being both necessary and sufficient for basolateral targeting of E-cadherin. Truncation mutants unable to bind beta -catenin were correctly targeted, showing, contrary to current understanding, that beta -catenin is not required for basolateral trafficking. Our results also provide evidence that dileucine-mediated targeting is maintained in LLC-PK1 cells despite the altered polarity of basolateral proteins with tyrosine-based signals in this cell line. These results provide the first direct insights into how E-cadherin is targeted to the basolateral membrane.

* This work was funded in part by grants from the National Health and Medical Research Council (to J. L. S. and A. S. Y.) and from the Australian Research Council as part of the Special Research Center for Functional Genomics.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.

** A Wellcome Trust International Senior Medical Research Fellow.

Dagger Dagger To whom correspondence should be addressed: Tel.: 61-7-3365-8242; Fax: 61-7-3665-4388; E-mail: r.teasdale@imb.uq.edu.au.

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