Regulation of endocytosis, nuclear translocation, and signaling of fibroblast growth factor receptor 1 by E-cadherin

Bryant, David M., Wylie, Fiona G. and Stow, Jennifer L. (2005) Regulation of endocytosis, nuclear translocation, and signaling of fibroblast growth factor receptor 1 by E-cadherin. Molecular Biology of The Cell, 16 1: 14-23. doi:10.1091/mbc.E04-09-0845

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Author Bryant, David M.
Wylie, Fiona G.
Stow, Jennifer L.
Title Regulation of endocytosis, nuclear translocation, and signaling of fibroblast growth factor receptor 1 by E-cadherin
Journal name Molecular Biology of The Cell   Check publisher's open access policy
ISSN 1059-1524
1939-4586
Publication date 2005
Sub-type Article (original research)
DOI 10.1091/mbc.E04-09-0845
Open Access Status File (Publisher version)
Volume 16
Issue 1
Start page 14
End page 23
Total pages 10
Place of publication Bethesda
Publisher American Society for Cell Biology
Collection year 2005
Language eng
Subject C1
270103 Protein Targeting and Signal Transduction
780106 Political science and public policy
Abstract Fibroblast growth factor (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 mitogen-activated protein kinase pathway. Furthermore, stabilization of surface adhesive E-cadherin, by overexpressing p120(ctn), 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.
Keyword Cell Biology
Cell-adhesion
Fgf-receptor
Epithelial-cells
Down-regulation
Breast-cancer
Beta-catenin
P120 Catenin
Pathway
Protein
Inhibition
Q-Index Code C1
Additional Notes 10.1091/mbc.E04-09-0845

 
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Created: Wed, 15 Aug 2007, 06:24:12 EST