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

Author

Listed:
  • Jen-Chih Hsieh

    (Johns Hopkins University School of Medicine
    Howard Hughes Medical Institute, 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
    Howard Hughes Medical Institute, Johns Hopkins University School of Medicine)

  • Philip M. Smallwood

    (Johns Hopkins University School of Medicine
    Howard Hughes Medical Institute, 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
    Howard Hughes Medical Institute, Johns Hopkins University School of Medicine
    Johns Hopkins University School of Medicine)

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.

Suggested Citation

  • Jen-Chih Hsieh & Laurent Kodjabachian & Martha L. Rebbert & Amir Rattner & Philip M. Smallwood & Cynthia Harryman Samos & Roel Nusse & Igor B. Dawid & Jeremy Nathans, 1999. "A new secreted protein that binds to Wnt proteins and inhibits their activites," Nature, Nature, vol. 398(6726), pages 431-436, April.
    • Handle: RePEc:nat:nature:v:398:y:1999:i:6726:d:10.1038_18899
    DOI: 10.1038/18899
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    Cited by:

    1. Jiawei Cai & Bohao Zhao & Jiali Li & Zhiyuan Bao & Yang Chen & Yan Liu & Xinsheng Wu, 2022. "A Single Nucleotide Polymorphism in the WIF1 Promoter Region Regulates the Wool Length in Rabbits," Agriculture, MDPI, vol. 12(11), pages 1-9, November.
    2. Hui Sun & Hui Li & Jie Yan & Xiangdong Wang & Mengyuan Xu & Mingxia Wang & Baozhen Fan & Jieying Liu & Ninghua Lin & Xin Wang & Li Li & Shengtian Zhao & Yongfeng Gong, 2022. "Loss of CLDN5 in podocytes deregulates WIF1 to activate WNT signaling and contributes to kidney disease," Nature Communications, Nature, vol. 13(1), pages 1-18, December.

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