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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7061
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pubmed:dateCreated |
2005-10-13
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Smo protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Veratrum Alkaloids,
http://linkedlifedata.com/resource/pubmed/chemical/cyclopamine,
http://linkedlifedata.com/resource/pubmed/chemical/smoothened protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1476-4687
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
13
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pubmed:volume |
437
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1018-21
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:16136078-Amino Acid Motifs,
pubmed-meshheading:16136078-Amino Acid Sequence,
pubmed-meshheading:16136078-Animals,
pubmed-meshheading:16136078-Caenorhabditis elegans,
pubmed-meshheading:16136078-Cell Line,
pubmed-meshheading:16136078-Cilia,
pubmed-meshheading:16136078-Dogs,
pubmed-meshheading:16136078-Drosophila Proteins,
pubmed-meshheading:16136078-Embryo, Mammalian,
pubmed-meshheading:16136078-Embryo, Nonmammalian,
pubmed-meshheading:16136078-Genes, Reporter,
pubmed-meshheading:16136078-Mice,
pubmed-meshheading:16136078-Mutation,
pubmed-meshheading:16136078-Protein Sorting Signals,
pubmed-meshheading:16136078-RNA, Messenger,
pubmed-meshheading:16136078-Receptors, G-Protein-Coupled,
pubmed-meshheading:16136078-Signal Transduction,
pubmed-meshheading:16136078-Veratrum Alkaloids,
pubmed-meshheading:16136078-Vertebrates,
pubmed-meshheading:16136078-Zebrafish
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pubmed:year |
2005
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pubmed:articleTitle |
Vertebrate Smoothened functions at the primary cilium.
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pubmed:affiliation |
Developmental and Stem Cell Biology Program, University of California, San Francisco, California 94143, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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