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First published online March 5, 2008
doi: 10.1242/10.1242/jcs.000455

Journal of Cell Science 121, 727-735 (2008)
Published by The Company of Biologists 2008
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Cadherin switching

Margaret J. Wheelock*, Yasushi Shintani, Masato Maeda, Yuri Fukumoto and Keith R. Johnson

University of Nebraska Medical Center, Department of Oral Biology and Eppley Cancer Center, Omaha, NE 68198-7696, USA


Figure 1
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  		Fig. 1. Mouse mammary epithelial cells undergo EMT in response to TGFβ1. (A,B) Phase micrographs of cells from the mouse mammary epithelial cell line NMuMG in the (A) absence or (B) presence of TGFβ1 (5 ng/ml for 1 day). (C,D) Cells were stained for filamentous actin with Texas-red-labeled phalloidin. (C) Untreated cells show a peripheral band of actin filaments, typical of polarized epithelial cells. (D) TGFβ1-treated cells have prominent stress fibers. Reproduced from Maeda et al. (Maeda et al., 2005Go).

 

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  		Fig. 2. Cadherin domain structure. Cadherins are single-pass transmembrane proteins that are synthesized with a signal peptide (SP) and pro-region (pro), which are removed during protein processing. The extracellular domain comprises five homologous repeats (EC1-EC5) that are bridged by calcium ions (Ca2+). The cytoplasmic domain binds to p120-catenin (p120ctn) near the plasma membrane and to β-catenin near the C-terminus. {alpha}-catenin binds to β-catenin to link the cadherin complex to the actin cytoskeleton. E-cadherin and N-cadherin domain structures are similar, as are their interactions with catenins.

 

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  		Fig. 3. p120-catenin promotes epithelial morphology in p120-deficient S2013 pancreatic cancer cells. Parental S2013 cells (wild type; WT) are scattered (A), whereas cells expressing p120-catenin form compact colonies of cobblestone-like cells (B).

 

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  		Fig. 4. Cadherin switching can influence many cellular activities. Shown are some of the changes in cellular behavior that can be induced by cadherin switching. N-cadherin interacts with the FGF receptor (FGFR) and stabilizes the receptor on the cell surface. N-cadherin increases tumor cell interactions with endothelial and mesenchymal cells. NHERF links N-cadherin to the PDGF receptor (PDGFR) via interactions with β-catenin in lamellipodia to increase cell motility. N-cadherin and R-cadherin increase steady-state levels of activated Rac and Cdc42, which promotes cell motility. N-cadherin and R-cadherin promote endocytosis of E-cadherin via competition for p120-catenin.

 




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