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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
1999-6-17
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pubmed:abstractText |
To understand the mechanism of how Axin acts as an inhibitory molecule in the Wnt pathway, we generated a series of mutated forms of Axin. From the binding experiments, we defined the domains of Axin that bind glycogen synthase kinase-3beta (GSK-3beta) and beta-catenin. We also examined the ability of each Axin mutant to inhibit lymphoid enhancer factor-1 (Lef-1) reporter activity in a cell line expressing high levels of beta-catenin. Axin mutants that did not bind GSK-3beta or beta-catenin were ineffective in suppressing Lef-1 reporter activity. Binding GSK-3beta and beta-catenin was not sufficient for this inhibitory effect of Axin. Axin mutants with C-terminal truncations lacked the ability to inhibit Lef-1 reporter activity, even though they bound GSK-3beta and beta-catenin. The C-terminal region was required for binding to Axin itself. Substitution of the C-terminal region with an unrelated dimerizing molecule, the retinoid X receptor restored its inhibitory effect on Lef-1-dependent transcription. The oligomerization of Axin through its C terminus is important for its function in regulation of beta-catenin-mediated response.
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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/Axin Protein,
http://linkedlifedata.com/resource/pubmed/chemical/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Catnb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/LEF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Lef1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphoid Enhancer-Binding Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14090-3
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10318824-Animals,
pubmed-meshheading:10318824-Axin Protein,
pubmed-meshheading:10318824-Binding Sites,
pubmed-meshheading:10318824-COS Cells,
pubmed-meshheading:10318824-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:10318824-Colonic Neoplasms,
pubmed-meshheading:10318824-Cytoskeletal Proteins,
pubmed-meshheading:10318824-DNA-Binding Proteins,
pubmed-meshheading:10318824-Glycogen Synthase Kinase 3,
pubmed-meshheading:10318824-Glycogen Synthase Kinases,
pubmed-meshheading:10318824-Humans,
pubmed-meshheading:10318824-Lymphoid Enhancer-Binding Factor 1,
pubmed-meshheading:10318824-Mice,
pubmed-meshheading:10318824-Mutagenesis, Site-Directed,
pubmed-meshheading:10318824-Protein Conformation,
pubmed-meshheading:10318824-Proteins,
pubmed-meshheading:10318824-Repressor Proteins,
pubmed-meshheading:10318824-Structure-Activity Relationship,
pubmed-meshheading:10318824-Trans-Activators,
pubmed-meshheading:10318824-Transcription, Genetic,
pubmed-meshheading:10318824-Transcription Factors,
pubmed-meshheading:10318824-Tumor Cells, Cultured,
pubmed-meshheading:10318824-beta Catenin
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pubmed:year |
1999
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pubmed:articleTitle |
Functional domains of axin. Importance of the C terminus as an oligomerization domain.
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pubmed:affiliation |
Cardiovascular Research Institute, University of California, San Francisco, California 94143-0130, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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