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Sci. STKE, 31 July 2007 PERSPECTIVESMolecular Scaffolds Regulate Bidirectional Crosstalk Between Wnt and Classical Seven-Transmembrane Domain Receptor Signaling PathwaysThomas Force1,2,3*, Kathleen Woulfe1,3, Walter J. Koch1, and Risto Kerkelä1
1The Center for Translational Medicine, Thomas Jefferson University, Philadelphia, PA 19107, USA. Abstract:
Signaling downstream of classical seven-transmembrane domain receptors (7TMRs) had generally been thought to recruit factors that are in large part separate from those recruited by atypical 7TMRs, such as Frizzleds (Fzs), receptors for the Wnt family of glycoproteins. Classical 7TMRs are also known as G protein–coupled receptors (GPCRs) and are mediated by signaling factors such as heterotrimeric guanine nucleotide–binding proteins (G proteins), GPCR kinases (GRKs), and *Corresponding author. E-mail: thomas.force{at}jefferson.edu
Citation: T. Force, K. Woulfe, W. J. Koch, R. Kerkelä, Molecular Scaffolds Regulate Bidirectional Crosstalk Between Wnt and Classical Seven-Transmembrane Domain Receptor Signaling Pathways. Sci. STKE 2007, pe41 (2007). THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882