Journal
NATURE COMMUNICATIONS
Volume 7, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms10909
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Funding
- Karlsruhe School of Optics and Photonics (KSOP)
- National Institutes of Health USPHS [F31-DE023275, RO1-DE016289]
- Deutsche Forschungsgemeinschaft (DFG) [WE-1208-13-1]
- 'Concept for the Future' programme of Karlsruhe Institute of Technology within the framework of the German Excellence Initiative
- 'Concept for the Future' of the KIT
- subproject E2.4 of the DFG-Center for Functional Nanostructures
- Deutsche Forschungsgemeinschaft (DFG) through the DFG-FOR 1756 program [KA 4104/1-2, FR 2107/2-1]
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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 beta 1-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.
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