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

Langhe, Rahul P. 1; Gudzenko, Tetyana 2; Bachmann, Michael 1; Becker, Sarah F. 1; Gonnermann, Carina 2; Winter, Claudia 1; Abbruzzese, Genevieve; Alfandari, Dominique; Kratzer, Marie-Claire 1,3; Franz, Clemens M. 2; Kashef, Jubin 1,4
1 Zoologisches Institut (ZOO), Karlsruher Institut für Technologie (KIT)
2 Center for Functional Nanostructures (CFN), Karlsruher Institut für Technologie (KIT)
3 Laboratorium für Applikationen der Synchrotronstrahlung (LAS), Karlsruher Institut für Technologie (KIT)
4 Institut für Photonenforschung und Synchrotronstrahlung (IPS), Karlsruher Institut für Technologie (KIT)

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.


Volltext §
DOI: 10.5445/IR/1000064165
Originalveröffentlichung
DOI: 10.1038/ncomms10909
Scopus
Zitationen: 54
Web of Science
Zitationen: 54
Dimensions
Zitationen: 64
Cover der Publikation
Zugehörige Institution(en) am KIT Center for Functional Nanostructures (CFN)
Institut für Photonenforschung und Synchrotronstrahlung (IPS)
Universität Karlsruhe (TH) – Interfakultative Einrichtungen (Interfakultative Einrichtungen)
Karlsruhe School of Optics & Photonics (KSOP)
Laboratorium für Applikationen der Synchrotronstrahlung (LAS)
Zoologisches Institut (ZOO)
Publikationstyp Zeitschriftenaufsatz
Publikationsjahr 2016
Sprache Englisch
Identifikator ISSN: 2041-1723
urn:nbn:de:swb:90-641652
KITopen-ID: 1000064165
Erschienen in Nature Communications
Verlag Nature Research
Band 7
Seiten Art.Nr.: 10909
Nachgewiesen in Dimensions
Web of Science
Scopus
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