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Am J Physiol Cell Physiol 297: C419-C429, 2009. First published May 27, 2009; doi:10.1152/ajpcell.00101.2009
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RECEPTORS AND SIGNAL TRANSDUCTION

DDR1/E-cadherin complex regulates the activation of DDR1 and cell spreading

Chau-Zen Wang,1 Yi-Chun Yeh,2 and Ming-Jer Tang2,3

1Department of Physiology, Kaohsiung Medical University, Kaohsiung, Taiwan; and 2Institute of Basic Medical Sciences and 3Department of Physiology, National Cheng-Kung University Medical College, Tainan, Taiwan

Submitted 6 March 2009 ; accepted in final form 26 May 2009

Discoidin domain receptors (DDRs) 1 and 2, collagen receptors, regulate cell adhesion and a broad range of cell behavior. Their adhesion-dependent regulation of signaling associated with adhesion proteins has not been elucidated. We report a novel mechanism: the cross talk of DDR1 and E-cadherin negatively and adhesion dependently regulated both DDR1 activity and DDR1-suppressed cell spreading. E-cadherin forms complexes with both DDR1 isoforms (a and b). E-cadherin regulates DDR1 activity associated with the cell-junction complexes formed between DDR1 and E-cadherin. These complexes are formed independently of DDR1 activation and of β-catenin and p120-catenin binding to E-cadherin; they are ubiquitous in epithelial cells. Small interfering RNA-mediated gene silencing of E-cadherin restores both DDR1 activity and DDR1-suppressed cell spreading and increases the apically and basally located DDR1 in E-cadherin-null cells. We conclude that E-cadherin-mediated adhesions decrease DDR1 activity, which subsequently eliminates DDR1-suppressed cell spreading, by sequestering DDR1 to cell junctions, which prevents its contact with collagen ligand.

discoidin domain receptor; collagen; Madin-Darby canine kidney cells


Address for reprint requests and other correspondence: M.-J. Tang, Dept. of Physiology, National Cheng-Kung Univ. Medical College, 1 Da-Hsueh Road, Tainan 701, Taiwan (e-mail: mjtang1{at}mail.ncku.edu.tw)






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