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A more recent version of this article appeared on April 13, 2001
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Papers In Press, published online ahead of print February 13, 2001
J. Biol. Chem, 10.1074/jbc.C100039200
Submitted on January 24, 2001
Revised on February 13, 2001
Accepted on February 13, 2001

FP prostanoid receptor activation of a Tcf/beta-catenin signaling pathway

Hiromichi Fujino and John W. Regan

Pharmacology & Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ 85721-0207

Corresponding Author: regan{at}pharmacy.arizona.edu

FP prostanoid receptors are G-protein coupled receptors (GPCR) that consist of two known isoforms named FPA and FPB. These isoforms, which are generated by alternative mRNA splicing, are identical except for their carboxyl terminal domains. Previously we have shown that stimulation of both isoforms with prostaglandin F2{alpha} (PGF2{alpha}) activates the small G-protein, Rho, leading to morphological changes consisting of cell rounding and the formation of cell aggregates. Following the removal of PGF2{alpha}, however, FPA expressing cells show rapid reversal of cell rounding, whereas FPB expressing cells do not. We now show that acute treatment of FPB expressing cells with PGF2{alpha} leads to a subcellular reorganization of beta -catenin, a decrease in the phosphorylation of cytoplasmic beta -catenin, and persistent stimulation of Tcf/Lef mediated transcriptional activation. This does not occur in FPA expressing cells and may underlie the differences between these isoforms with respect to the reversal of cell rounding. The Tcf/beta -catenin signaling pathway is known to mediate the actions of Wnt acting through the heptahelical receptor, Frizzled, and has not been previously associated with GPCR activation. Our findings expand the signaling possibilities for GPCRs and suggest novel roles for FP receptors in normal tissue development and malignant transformation.


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