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A more recent version of this article appeared on January 1, 2005
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Submitted on September 27, 2004
Accepted on October 14, 2004
*Institute for Molecular Bioscience and School of Molecular and Microbial Science, The University of Queensland, Brisbane, Australia 4072
Monitoring Editor: Suzanne Pfeffer
FGF receptors (FGFRs) signal to modulate diverse cellular functions including epithelial cell morphogenesis. In epithelial cells, E-cadherin plays a key role in cell-cell adhesion, and its function can be regulated through endocytic trafficking. In this study we investigated the location, trafficking and function of FGFR1 and E-cadherin and report a novel mechanism, based on endocytic trafficking, for the coregulation of E-cadherin and signaling from FGFR1. FGF induces the internalization of surface FGFR1 and surface E-cadherin, followed by nuclear translocation of FGFR1. The internalization of both proteins is regulated by common endocytic machinery, resulting in cointernalization of FGFR1 and E-cadherin into early endosomes. By blocking endocytosis we show that this is a requisite, initial step for the nuclear translocation of FGFR1. Overexpression of E-cadherin blocks both the coendocytosis of E-cadherin and FGFR1, the nuclear translocation of FGFR1 and FGF-induced signaling to the MAPK pathway. Furthermore, stabilization of surface adhesive E-cadherin, by overexpressing p120ctn, also blocks internalization and nuclear translocation of FGFR1. These data reveal that conjoint endocytosis and trafficking is a novel mechanism for the coregulation of E-cadherin and FGFR1 during cell signaling and morphogenesis.
Corresponding author.
E-mail: j.stow{at}imb.uq.edu.au
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