LDL-receptor-related proteins in Wnt signal transduction

Keiko Tamai, Mikhail Semenov, Yoichi Kato, Rebecca Spokony, Chunming Liu, Yu Katsuyama, Fred Hess, Jean-Pierre Saint-Jeannet and Xi He ()
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Keiko Tamai: Children's Hospital, Harvard Medical School
Mikhail Semenov: Children's Hospital, Harvard Medical School
Yoichi Kato: Children's Hospital, Harvard Medical School
Rebecca Spokony: School of Veterinary Medicine, University of Pennsylvania
Chunming Liu: Children's Hospital, Harvard Medical School
Yu Katsuyama: Children's Hospital, Harvard Medical School
Fred Hess: Merck Research Laboratories
Jean-Pierre Saint-Jeannet: School of Veterinary Medicine, University of Pennsylvania
Xi He: Children's Hospital, Harvard Medical School

Nature, 2000, vol. 407, issue 6803, 530-535

Abstract: Abstract The Wnt family of secreted signalling molecules are essential in embryo development and tumour formation1. The Frizzled (Fz) family of serpentine receptors function as Wnt receptors2,3,4,5,6,7,8,9,10, but how Fz proteins transduce signalling is not understood. In Drosophila , arrow phenocopies the wingless (DWnt-1) phenotype11, and encodes a transmembrane protein11 that is homologous to two members of the mammalian low-density lipoprotein receptor (LDLR)-related protein (LRP) family, LRP5 and LRP6 (refs 12,13,14, 15). Here we report that LRP6 functions as a co-receptor for Wnt signal transduction. In Xenopus embryos, LRP6 activated Wnt–Fz signalling, and induced Wnt responsive genes, dorsal axis duplication and neural crest formation. An LRP6 mutant lacking the carboxyl intracellular domain blocked signalling by Wnt or Wnt–Fz, but not by Dishevelled or β-catenin, and inhibited neural crest development. The extracellular domain of LRP6 bound Wnt-1 and associated with Fz in a Wnt-dependent manner. Our results indicate that LRP6 may be a component of the Wnt receptor complex.

Date: 2000
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DOI: 10.1038/35035117

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