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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2006-4-11
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pubmed:abstractText |
Dishevelled is a conserved protein that interprets signals received by Frizzled receptors. Using a tandem-affinity purification strategy and mass spectrometry we have identified proteins associated with Dishevelled, including a Cullin-3 ubiquitin ligase complex containing the Broad Complex, Tramtrack and Bric à Brac (BTB) protein Kelch-like 12 (KLHL12). This E3 ubiquitin ligase complex is recruited to Dishevelled in a Wnt-dependent manner that promotes its poly-ubiquitination and degradation. Functional analyses demonstrate that regulation of Dishevelled by this ubiquitin ligase antagonizes the Wnt-beta-catenin pathway in cultured cells, as well as in Xenopus and zebrafish embryos. Considered with evidence that the distinct Cullin-1 based SCF(beta-TrCP)complex regulates beta-catenin stability, our data on the stability of Dishevelled demonstrates that two distinct ubiquitin ligase complexes regulate the Wnt-beta-catenin pathway.
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pubmed:grant |
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/CUL3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cullin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Wnt Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Zebrafish Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/dishevelled proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1465-7392
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
348-57
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16547521-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:16547521-Animals,
pubmed-meshheading:16547521-Blotting, Western,
pubmed-meshheading:16547521-Carrier Proteins,
pubmed-meshheading:16547521-Cell Cycle Proteins,
pubmed-meshheading:16547521-Cell Line,
pubmed-meshheading:16547521-Chromatography, Affinity,
pubmed-meshheading:16547521-Cullin Proteins,
pubmed-meshheading:16547521-Embryo, Nonmammalian,
pubmed-meshheading:16547521-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:16547521-Humans,
pubmed-meshheading:16547521-Kidney,
pubmed-meshheading:16547521-Microscopy, Fluorescence,
pubmed-meshheading:16547521-Phosphoproteins,
pubmed-meshheading:16547521-Signal Transduction,
pubmed-meshheading:16547521-Ubiquitin,
pubmed-meshheading:16547521-Ubiquitin-Protein Ligases,
pubmed-meshheading:16547521-Wnt Proteins,
pubmed-meshheading:16547521-Xenopus Proteins,
pubmed-meshheading:16547521-Xenopus laevis,
pubmed-meshheading:16547521-Zebrafish,
pubmed-meshheading:16547521-Zebrafish Proteins,
pubmed-meshheading:16547521-beta Catenin
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pubmed:year |
2006
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pubmed:articleTitle |
The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation.
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pubmed:affiliation |
Howard Hughes Medical Institute, University of Washington School of Medicine, Box 357370, Seattle, WA 98195, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, N.I.H., Extramural
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