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Dual roles for patched in sequestering and transducing hedgehog
Author(s): Chen Y, Struhl G
Source: CELL    Volume: 87    Issue: 3    Pages: 553-563    Published: NOV 1 1996  
Times Cited: 444     References: 51     
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.
Document Type: Article
Language: English
Reprint Address: Chen, Y (reprint author), COLUMBIA UNIV COLL PHYS & SURG, HOWARD HUGHES MED INST, DEPT GENET & DEV, NEW YORK, NY 10032 USA
Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: VQ466
ISSN: 0092-8674
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