Cadherin-11 localizes to focal adhesions and promotes cell–substrate adhesion

Rahul P. Langhe, Tetyana Gudzenko, Michael Bachmann, Sarah F. Becker, Carina Gonnermann, Claudia Winter, Genevieve Abbruzzese, Dominique Alfandari, Marie-Claire Kratzer, Clemens M. Franz () and Jubin Kashef ()
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Rahul P. Langhe: Zoological Institute, Cell and Developmental Biology, Karlsruhe Institute of Technology (KIT)
Tetyana Gudzenko: Center for Functional Nanostructures, Karlsruhe Institute of Technology (KIT)
Michael Bachmann: Zoological Institute, Cell and Neurobiology Biology, Karlsruhe Institute of Technology (KIT)
Sarah F. Becker: Zoological Institute, Cell and Developmental Biology, Karlsruhe Institute of Technology (KIT)
Carina Gonnermann: Center for Functional Nanostructures, Karlsruhe Institute of Technology (KIT)
Claudia Winter: Zoological Institute, Cell and Developmental Biology, Karlsruhe Institute of Technology (KIT)
Genevieve Abbruzzese: University of Massachusetts
Dominique Alfandari: University of Massachusetts
Marie-Claire Kratzer: Zoological Institute, Cell and Developmental Biology, Karlsruhe Institute of Technology (KIT)
Clemens M. Franz: Center for Functional Nanostructures, Karlsruhe Institute of Technology (KIT)
Jubin Kashef: Zoological Institute, Cell and Developmental Biology, Karlsruhe Institute of Technology (KIT)

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: Abstract Cadherin receptors have a well-established role in cell–cell adhesion, cell polarization and differentiation. However, some cadherins also promote cell and tissue movement during embryonic development and tumour progression. In particular, cadherin-11 is upregulated during tumour and inflammatory cell invasion, but the mechanisms underlying cadherin-11 stimulated cell migration are still incompletely understood. Here, we show that cadherin-11 localizes to focal adhesions and promotes adhesion to fibronectin in Xenopus neural crest, a highly migratory embryonic cell population. Transfected cadherin-11 also localizes to focal adhesions in different mammalian cell lines, while endogenous cadherin-11 shows focal adhesion localization in primary human fibroblasts. In focal adhesions, cadherin-11 co-localizes with β1-integrin and paxillin and physically interacts with the fibronectin-binding proteoglycan syndecan-4. Adhesion to fibronectin mediated by cadherin-11/syndecan-4 complexes requires both the extracellular domain of syndecan-4, and the transmembrane and cytoplasmic domains of cadherin-11. These results reveal an unexpected role of a classical cadherin in cell–matrix adhesion during cell migration.

Date: 2016
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DOI: 10.1038/ncomms10909

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