TY - JOUR T1 - Enhanced cell-cell contact stability and decreased N-cadherin-mediated migration upon Fibroblast Growth Factor Receptor-N-cadherin cross-talk JF - bioRxiv DO - 10.1101/465930 SP - 465930 AU - Thao Nguyen AU - Laurence Duchesne AU - Gautham Hari Narayana Sankara Narayana AU - Nicole Boggetto AU - David D. Fernig AU - Chandrashekhar Uttamrao Murade AU - Benoit Ladoux AU - René-Marc Mège Y1 - 2019/01/01 UR - http://biorxiv.org/content/early/2019/06/17/465930.abstract N2 - N-cadherin adhesion has been reported to enhance cancer and neuronal cell migration either by mediating actomyosin-based force transduction or initiating Fibroblast Growth Factor Receptor (FGFR)-dependent biochemical signalling. Here we show that FGFR1 reduces N-cadherin-mediated cell migration. Both proteins are co-stabilised at cell-cell contacts through direct interaction. As a consequence, cell adhesion is strengthened, limiting the migration of cells on N-cadherin. Both the inhibition of migration and the stabilisation of cell adhesions require the FGFR activity stimulated by N-cadherin engagement. FGFR1 stabilises N-cadherin at the cell membrane through a pathway involving Src and p120. Moreover, FGFR1 stimulates the anchoring of N-cadherin to actin. We found that the migratory behaviour of cells depends on an optimum balance between FGFR-regulated N-cadherin adhesion and actin dynamics. Based on these findings we propose a positive feedback loop between N-cadherin and FGFR at adhesion sites limiting N-cadherin-based single cell migration.FGFFibroblast Growth FactorFGFRFibroblast Growth Factor ReceptorFPFluorescent ProteinFNFibronectinFRAPFluorescence Recovery After PhotobleachingGFPGreen Fluorescent ProteinNcadN-cadherinPBSPhosphate Buffer SalineRTKReceptor Tyrosine KinaseSEMStandard Error of the Mean ER -