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Protein A003905
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Published 11 Jan 2010
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UCSD-Nature Molecule Pages
Published online: 11 Jan 2010 | doi:10.1038/mp.a003905.01

E-cadherin

Karl-Friedrich Becker1, Birgit Luber1

1Institut fuer Pathologie, Technische Universitaet Muenchen, 81675 Muenchen, DE.

Correspondence should be addressed to Karl-Friedrich Becker: kf.becker@lrz.tum.de


Among the various classes of molecules involved in cell-cell interactions, cadherins form a group of calcium-dependent transmembrane glycoproteins that typically mediate homophilic and homotypic cell-cell adhesion. One of the earliest and most extensively analyzed molecules of the cadherin superfamily is E-cadherin, a cell surface protein preferentially expressed on epithelial cells of a variety of tissues in different species. E-cadherin has a crucial role in many aspects of cell adhesion, epithelial development, and establishment and maintenance of epithelial polarity. Loss of the adhesive function of E-cadherin is a crucial step in the promotion of epithelial cells to a more malignant phenotype, facilitating invasion and metastasis of epithelial tumors. Specifically, protein-truncating germline mutations in CDH1, the gene encoding E-cadherin, confer a high risk of diffuse gastric cancer, with the gene acting as a classic tumor suppressor.

Alternative names for this molecule: Cadherin 1; Cdh1; E-cadherin; Ecad; Um; Uvo; uvomorulin

Transition Network Graph This molecule exists in 33 states, has 38 transitions between these states and has 1 receptor function.

[map] View high resolution network map

Acknowledgments: This contribution was supported by Deutsche Forschungsgemeinschaft SFB456 to BL, Deutsche Krebshilfe grant number 106947 to KFB, and Deutsche Krebshilfe grant number 106148 to BL.

 

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