Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Sci. STKE, 31 July 2007
Vol. 2007, Issue 397, p. pe41
[DOI: 10.1126/stke.3972007pe41]

PERSPECTIVES

Molecular Scaffolds Regulate Bidirectional Crosstalk Between Wnt and Classical Seven-Transmembrane Domain Receptor Signaling Pathways

Thomas Force1,2,3*, Kathleen Woulfe1,3, Walter J. Koch1, and Risto Kerkelä1

1The Center for Translational Medicine, Thomas Jefferson University, Philadelphia, PA 19107, USA.
2Cardiology Division, Thomas Jefferson University, Philadelphia, PA 19107, USA.
3Program in Cell and Developmental Biology, 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 beta-arrestins. Over the past few years, it has become increasingly apparent that classical and atypical 7TMRs share these factors, which are often associated with mediating classical 7TMR signaling, as well as the scaffolding proteins that were initially thought to be involved in transmitting atypical 7TMR signals. This sharing of signaling components by agonists that bind classical 7TMRs and those binding to atypical 7TMRs establishes the possibility of extensive crosstalk between these receptor classes. We discuss the evidence for, and against, crosstalk, and examine mechanisms by which this can occur.

*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).

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Arrestins 2 and 3 differentially regulate ETA and P2Y2 receptor-mediated cell signaling and migration in arterial smooth muscle.
G. E. Morris, C. P. Nelson, P. J. Brighton, N. B. Standen, R. A. J. Challiss, and J. M. Willets (2012)
Am J Physiol Cell Physiol 302, C723-C734
   Abstract »    Full Text »    PDF »
Phosphatidylinositol 3-Kinase Facilitates Microtubule-dependent Membrane Transport for Neuronal Growth Cone Guidance.
H. Akiyama and H. Kamiguchi (2010)
J. Biol. Chem. 285, 41740-41748
   Abstract »    Full Text »    PDF »
International Union of Basic and Clinical Pharmacology. LXXX. The Class Frizzled Receptors.
G. Schulte (2010)
Pharmacol. Rev. 62, 632-667
   Abstract »    Full Text »    PDF »
WNT Signaling in Adult Cardiac Hypertrophy and Remodeling: Lessons Learned From Cardiac Development.
M. W. Bergmann (2010)
Circ. Res. 107, 1198-1208
   Abstract »    Full Text »    PDF »
The G protein-coupled receptor T-cell death-associated gene 8 (TDAG8) facilitates tumor development by serving as an extracellular pH sensor.
Y. Ihara, Y. Kihara, F. Hamano, K. Yanagida, Y. Morishita, A. Kunita, T. Yamori, M. Fukayama, H. Aburatani, T. Shimizu, et al. (2010)
PNAS 107, 17309-17314
   Abstract »    Full Text »    PDF »

To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882