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EMBO reports 7, 3, 283–290 (2006)
doi:10.1038/sj.embor.7400614
AOP Published online: 20 January 2006
A role for fibronectin-leucine-rich transmembrane cell-surface proteins in homotypic cell adhesion
Emil E Karaulanov*, Ralph T Böttcher*† & Christof Niehrs
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Division of Molecular Embryology, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany
To whom correspondence should be addressed
Christof Niehrs Tel: +49 6221 42 4690; Fax: +49 6221 42 4692; E-mail: niehrs@dkfz-heidelberg.de
* These authors contributed equally to this work
† Present address: Department of Molecular, Cellular and Developmental Biology, Yale University, Kline Biology Tower-244, 266 Whitney Avenue, New Haven, Connecticut 06511, USA
Received 4 July 2005; Accepted 23 November 2005; Published online 20 January 2006.
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Abstract
The fibronectin-leucine-rich transmembrane (FLRT) family of leucine-rich repeat (LRR) proteins is implicated in fibroblast growth factor (FGF) signalling, early embryonic development and neurite outgrowth. Here, we have analysed whether FLRTs may also function in cell adhesion. We find that FLRT proteins can physically interact and that FLRT-transfected cultured cells sort out from non-transfected cells, suggesting a change in adhesive properties. A similar sorting effect is also observed in Xenopus embryos and tissue aggregates. FLRT-mediated cell sorting is calcium dependent and substrate independent. Deletion analysis indicates that cell sorting requires the LRR domains, which are dispensable for FLRT-mediated FGF signalling. Conversely, sorting is independent of the cytoplasmic domain, which is essential for FLRT-induced signalling. Therefore, FLRT-mediated FGF signal transduction and homotypic cell sorting can be molecularly uncoupled. The results indicate that FLRT proteins have a dual role, promoting FGF signalling and modulating homotypic cell adhesion.
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