A new secreted protein that binds to Wnt proteins and inhibits their activites

Jen-Chih Hsieh, Laurent Kodjabachian, Martha L. Rebbert, Amir Rattner, Philip M. Smallwood, Cynthia Harryman Samos, Roel Nusse, Igor B. Dawid and Jeremy Nathans ()
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Jen-Chih Hsieh: Johns Hopkins University School of Medicine
Laurent Kodjabachian: Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, National Institutes of Health
Martha L. Rebbert: Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, National Institutes of Health
Amir Rattner: Johns Hopkins University School of Medicine
Philip M. Smallwood: Johns Hopkins University School of Medicine
Cynthia Harryman Samos: Howard Hughes Medical Institute, Stanford University School of Medicine
Roel Nusse: Howard Hughes Medical Institute, Stanford University School of Medicine
Igor B. Dawid: Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, National Institutes of Health
Jeremy Nathans: Johns Hopkins University School of Medicine

Nature, 1999, vol. 398, issue 6726, 431-436

Abstract: Abstract The Wnt proteins constitute a large family of extracellular signalling molecules that are found throughout the animal kingdom and are important for a wide variety of normal and pathological developmental processes1,2. Here we describe Wnt-inhibitory factor-1 (WIF-1), a secreted protein that binds to Wnt proteins and inhibits their activities. WIF-1 is present in fish, amphibia and mammals, and is expressed during Xenopus and zebrafish development in a complex pattern that includes paraxial presomitic mesoderm, notochord, branchial arches and neural crest derivatives. We use Xenopus embryos to show that WIF-1 overexpression affects somitogenesis (the generation of trunk mesoderm segments), in agreement with its normal expression in paraxial mesoderm. In vitro, WIF-1 binds to Drosophila Wingless and Xenopus Wnt8 produced by Drosophila S2 cells. Together with earlier results obtained with the secreted Frizzled-related proteins1,2, our results indicate that Wnt proteins interact with structurally diverse extracellular inhibitors, presumably to fine-tune the spatial and temporal patterns of Wnt activity.

Date: 1999
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DOI: 10.1038/18899

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