A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Reference Report

Reference
Citation Chen, Y., Struhl, G. (1996). Dual roles for Patched in sequestering and transducing Hedgehog.  Cell 87(3): 553--563. (Export to RIS)
FlyBase ID FBrf0090495
Publication Type Research paper
PubMed ID 8898207
PubMed 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.
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Language of Publication English
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Publication Type Journal
Abbreviation Cell
Title Cell
Publication Year 1974-
ISBN/ISSN 0092-8674
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