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Articles in PresS, published online ahead of print May 17, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00372.2001
Submitted on September 19, 2001
Accepted on April 25, 2002
1 Center for Craniofacial Biology, University Southern California, Los Aneles, CA, USA
2 Equipe Morphogenesis Cellulaire et Tumorale, Institut Curie, Paris, France, France; Equipe Morphogenesis Cellulaire et Tumorale, Institut Curie, Paris, France, France
* To whom correspondence should be addressed. E-mail: dwarburton{at}chla.usc.edu.
Murine Sprouty2 (mSpry2) is a conserved orthologue of Drosophila Sprouty, a gene that inhibits several tyrosine-kinase receptor pathways, resulting in net reduction of MAP-kinase activation. However, the precise mechanism mediating mSpry2 function as a negative regulator in tyrosine-kinase growth factor pathways that regulate diverse biological functions remains incompletely characterized. Fibroblast Growth Factor 10 (FGF10) is a key positive regulator of lung branching morphogenesis and induces epithelial expression of mSpry2 adjacent to mesenchymal sites of FGF10. Herein, we demonstrate that FGF10 stimulation of mouse lung epithelial cells (MLE15) overexpressing mSpry2 results in both mSpry2 tyrosine phosphorylation and differential binding of mSpry2 to several key upstream target proteins in the MAP-kinase activating pathway. Thus, FGFR activation respectively results in increased association of mSpry2 with Grb2, FRS2 and with Raf, but decreased binding to Shp2 and Gap1, resulting in a net reduction of MAP-kinase activation. mSpry2 also spatially translocates to the plasma membrane and intracellular membrane structures in response to FGF10 stimulation. Our data demonstrate novel intracellular mechanisms mediating mSpry2 function as a negative regulator of uncontrolled FGF induced MAP-kinase signaling.
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