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Vol. 16, Issue 4, 1744-1755, April 2005
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* Institute for Molecular Bioscience, The University of Queensland, Brisbane, 4072 Australia;
School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, 4072 Australia
Submitted October 5, 2004;
Revised January 13, 2005;
Accepted January 19, 2005
Monitoring Editor: Jennifer Lippincott-Schwartz
E-cadherin plays an essential role in cell polarity and cell-cell adhesion; however, the pathway for delivery of E-cadherin to the basolateral membrane of epithelial cells has not been fully characterized. We first traced the post-Golgi, exocytic transport of GFP-tagged E-cadherin (Ecad-GFP) in unpolarized cells. In live cells, Ecad-GFP was found to exit the Golgi complex in pleiomorphic tubulovesicular carriers, which, instead of moving directly to the cell surface, most frequently fused with an intermediate compartment, subsequently identified as a Rab11-positive recycling endosome. In MDCK cells, basolateral targeting of E-cadherin relies on a dileucine motif. Both E-cadherin and a targeting mutant, 
S1-E-cadherin, colocalized with Rab11 and fused with the recycling endosome before diverging to basolateral or apical membranes, respectively. In polarized and unpolarized cells, coexpression of Rab11 mutants disrupted the cell surface delivery of E-cadherin and caused its mistargeting to the apical membrane, whereas apical S1-E-cadherin was unaffected. We thus demonstrate a novel pathway for Rab11 dependent, dileucine-mediated, µ1B-independent sorting and basolateral trafficking, exemplified by E-cadherin. The recycling endosome is identified as an intermediate compartment for the post-Golgi trafficking and exocytosis of E-cadherin, with a potentially important role in establishing and maintaining cadherin-based adhesion.
Abbreviations used: AP, adaptor protein (complex); ctn, catenin; mRFP, monomeric red fluorescent protein; GGA, Golgi-localized, gamma ear-containing, ADP ribosylation factor-binding protein; LDLR, low-density lipoprotein receptor; MDCK, Madin-Darby canine kidney; PGC, post-Golgi carrier; PM, plasma membrane; SNARE, soluble N-ethyl maleimide–sensitive factor [NSF] attachment protein [SNAP] receptor; TGN, trans-Golgi network; VSVG, vesicular stomatitis virus glycoprotein.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Address correspondence to: Jennifer L. Stow (j.stow{at}imb.uq.edu.au).
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