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Science 14 March 1997: Vol. 275. no. 5306, pp. 1652 - 1654 DOI: 10.1126/science.275.5306.1652
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Reports
A Member of the Frizzled Protein Family Mediating Axis Induction by Wnt-5A
Xi He,
*
Jean-Pierre Saint-Jeannet,
Yanshu Wang,
Jeremy Nathans,
Igor Dawid,
Harold Varmus
In Xenopus laevis embryos, the Wingless/Wnt-1 subclass
of Wnt molecules induces axis duplication, whereas the Wnt-5A subclass does not. This difference could be explained by distinct signal transduction pathways or by a lack of one or more Wnt-5A receptors during axis formation. Wnt-5A induced axis duplication and an ectopic
Spemann organizer in the presence of hFz5, a member of the Frizzled
family of seven-transmembrane receptors. Wnt-5A/hFz5 signaling was
antagonized by glycogen synthase kinase-3 and by the amino-terminal
ectodomain of hFz5. These results identify hFz5 as a receptor for
Wnt-5A.
X. He and H. Varmus, National Cancer Institute, Building 49, Room
4A56, National Institutes of Health, Bethesda, MD 20892, USA.
J.-P. Saint-Jeannet and I. Dawid, National Institute of Child Health
and Human Development, National Institutes of Health, Bethesda, MD
20892, USA.
Y. Wang and J. Nathans, Howard Hughes Medical Institute, Department of
Molecular Biology and Genetics, The Johns Hopkins University School of
Medicine, Baltimore, MD 21205, USA.
X. He and H. Varmus, National Cancer Institute, Building 49, Room
4A56, National Institutes of Health, Bethesda, MD 20892, USA.
J.-P. Saint-Jeannet and I. Dawid, National Institute of Child Health
and Human Development, National Institutes of Health, Bethesda, MD
20892, USA.
Y. Wang and J. Nathans, Howard Hughes Medical Institute, Department of
Molecular Biology and Genetics, The Johns Hopkins University School of
Medicine, Baltimore, MD 21205, USA.
*
Present address: Division of Neuroscience, Enders 379, Children's Hospital/Harvard Medical School, 300 Longwood Avenue,
Boston, MA 02115, USA
To whom correspondence should be addressed. E-mail:
xhe{at}nhgri.nih.gov
Read the Full Text
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- Wnt signaling promotes oncogenic transformation by inhibiting c-Myc-induced apoptosis.
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