@article {140,
	title = {Dual roles for patched in sequestering and transducing Hedgehog.},
	journal = {Cell},
	volume = {87},
	year = {1996},
	month = {1996 Nov 1},
	pages = {553-63},
	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.},
	keywords = {Alleles, Animals, Animals, Genetically Modified, Drosophila melanogaster, Drosophila Proteins, Gene Expression Regulation, Developmental, Hedgehog Proteins, Insect Hormones, Insect Proteins, Macromolecular Substances, Membrane Proteins, Models, Biological, Multigene Family, Proteins, Receptors, Cell Surface, Receptors, G-Protein-Coupled, Signal Transduction, Wing},
	issn = {0092-8674},
	author = {Chen, Y and Struhl, G}
}
