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      Vertebrate Smoothened functions at the primary cilium.

      Nature

      metabolism, Amino Acid Motifs, genetics, embryology, Zebrafish, Vertebrates, pharmacology, Veratrum Alkaloids, Signal Transduction, chemistry, antagonists & inhibitors, Receptors, G-Protein-Coupled, RNA, Messenger, physiology, Protein Sorting Signals, Mutation, Mice, Genes, Reporter, Embryo, Nonmammalian, Embryo, Mammalian, Drosophila Proteins, Dogs, drug effects, Cilia, Cell Line, Caenorhabditis elegans, Animals, Amino Acid Sequence

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          Abstract

          The unanticipated involvement of several intraflagellar transport proteins in the mammalian Hedgehog (Hh) pathway has hinted at a functional connection between cilia and Hh signal transduction. Here we show that mammalian Smoothened (Smo), a seven-transmembrane protein essential for Hh signalling, is expressed on the primary cilium. This ciliary expression is regulated by Hh pathway activity; Sonic hedgehog or activating mutations in Smo promote ciliary localization, whereas the Smo antagonist cyclopamine inhibits ciliary localization. The translocation of Smo to primary cilia depends upon a conserved hydrophobic and basic residue sequence homologous to a domain previously shown to be required for the ciliary localization of seven-transmembrane proteins in Caenorhabditis elegans. Mutation of this domain not only prevents ciliary localization but also eliminates Smo activity both in cultured cells and in zebrafish embryos. Thus, Hh-dependent translocation to cilia is essential for Smo activity, suggesting that Smo acts at the primary cilium.

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          Journal
          16136078
          10.1038/nature04117

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