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Dual Roles for Patched in Sequestering and Transducing Hedgehog
Open accessAbstract
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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Metadata
- Authors
- Chen, Y., & Struhl, G.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1996-11
- Volume
- 87
- Issue
- 3
- Pages
- 553-563
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2028497134
- Cited by
- 900
- References
- 0
- FWCI
- 14.47
- Type
- journal article
- Language
- en
- Open access
- hybrid
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