Abstract
Secreted proteins of the Hedgehog (Hh) family have diverse organizing roles in animal development. Recently, a serpentine protein Smoothened (Smo) has been proposed as a Hh receptor. Here, we present evidence that implicates another multiple-pass transmembrane protein, Patched (Ptc), in Hh reception and suggests a novel signal transduction mechanism in which Hh binds to Ptc, or a Ptc-Smo complex, and thereby induces Smo activity. Our results also show that Ptc limits the range of Hh action; we provide evidence that high levels of Ptc induced by Hh serve to sequester any free Hh and therefore create a barrier to its further movement.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alleles
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Animals
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Animals, Genetically Modified
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Drosophila Proteins*
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Drosophila melanogaster / embryology
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Drosophila melanogaster / genetics*
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Drosophila melanogaster / growth & development
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Gene Expression Regulation, Developmental
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Hedgehog Proteins
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Insect Hormones / genetics
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Insect Hormones / physiology*
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Insect Proteins / physiology
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Macromolecular Substances
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Membrane Proteins / genetics
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Membrane Proteins / physiology*
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Models, Biological
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Multigene Family
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Proteins / genetics
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Proteins / metabolism*
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Receptors, Cell Surface / genetics
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Receptors, Cell Surface / physiology*
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Receptors, G-Protein-Coupled*
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Signal Transduction / physiology*
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Smoothened Receptor
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Wings, Animal / abnormalities
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Wings, Animal / embryology
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Wings, Animal / growth & development
Substances
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Drosophila Proteins
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Hedgehog Proteins
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Insect Hormones
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Insect Proteins
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Macromolecular Substances
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Membrane Proteins
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Proteins
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Receptors, Cell Surface
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Receptors, G-Protein-Coupled
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Smoothened Receptor
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dpp protein, Drosophila
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ptc protein, Drosophila
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smo protein, Drosophila
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hh protein, Drosophila