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Interaction of Wnt and a Frizzled homologue triggers G-protein-linked phosphatidylinositol signalling

Author

Listed:
  • Diane C. Slusarski

    (The Johns Hopkins University)

  • Victor G. Corces

    (The Johns Hopkins University)

  • Randall T. Moon

    (University of Washington School of Medicine)

Abstract

In Drosophila , members of the frizzled family of tissue-polarity genes encode proteins that are likely to function as cell-surface receptors of the type known as Wnt receptors, and to initiate signal transduction across the cell membrane1,2, although how they do this is unclear. We show here that the rat protein Frizzled-2 causes an increase in the release of intracellular calcium which is enhanced by Xwnt-5a, a member of the Wnt family. This release of intracellular calcium is suppressed by an inhibitor of the enzyme inositol monophosphatase and hence of the phosphatidylinositol signalling pathway; this suppression can be rescued by injection of the compound myo -inositol, which overcomes the decrease in this intermediate caused by the inhibitor. Agents that inhibit specific G-protein subunits, pertussis toxin, GDP-β-S and α-transducin also inhibit the calcium release triggered by Xwnt-5a and rat Frizzled-2. Our results indicate that some Wnt proteins work through specific Frizzled homologues to stimulate the phosphatidylinositol signalling pathway via heterotrimeric G-protein subunits.

Suggested Citation

  • Diane C. Slusarski & Victor G. Corces & Randall T. Moon, 1997. "Interaction of Wnt and a Frizzled homologue triggers G-protein-linked phosphatidylinositol signalling," Nature, Nature, vol. 390(6658), pages 410-413, November.
    • Handle: RePEc:nat:nature:v:390:y:1997:i:6658:d:10.1038_37138
    DOI: 10.1038/37138
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    1. Lukas Grätz & Maria Kowalski-Jahn & Magdalena M. Scharf & Pawel Kozielewicz & Michael Jahn & Julien Bous & Nevin A. Lambert & David E. Gloriam & Gunnar Schulte, 2023. "Pathway selectivity in Frizzleds is achieved by conserved micro-switches defining pathway-determining, active conformations," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

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