A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells

Miranda, Kevin C., Khromykh, Tatiana, Christy, Perpetina, Le, Tam Luan, Gottardi, Cara J., Yap, Alpha S., Stow, Jennifer L. and Teasdale, Rohan D. (2001) A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells. Journal of Biological Chemistry, 276 25: 22565-22572. doi:10.1074/jbc.M101907200

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Author Miranda, Kevin C.
Khromykh, Tatiana
Christy, Perpetina
Le, Tam Luan
Gottardi, Cara J.
Yap, Alpha S.
Stow, Jennifer L.
Teasdale, Rohan D.
Title A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2001-06-22
Year available 2001
Sub-type Article (original research)
DOI 10.1074/jbc.M101907200
Open Access Status File (Publisher version)
Volume 276
Issue 25
Start page 22565
End page 22572
Total pages 8
Editor H. Tabor
Place of publication USA
Publisher American Soc. for Biochemistry & Molecular Biology, Inc.
Language eng
Subject C1
270103 Protein Targeting and Signal Transduction
780105 Biological sciences
Abstract 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 ectodo- main of the interleukin-2 alpha (IL-2 alpha) 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 UC-PK, 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.
Keyword Biochemistry & Molecular Biology
Trans-golgi Network
Di-leucine Motif
Mdck Cells
Sorting Signals
Adhesion Molecule
Structural Requirements
Cytoplasmic Domain
Complex-formation
Catenin Complex
Plasma-membrane
Q-Index Code C1
Additional Notes DOI: 10.1074/jbc.M101907200

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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Created: Wed, 15 Aug 2007, 02:49:58 EST