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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2004-2-12
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pubmed:abstractText |
The identities of the ubiquitin-ligases active during myogenesis are largely unknown. Here we describe a RING-type E3 ligase complex specified by the adaptor protein, Ozz, a novel SOCS protein that is developmentally regulated and expressed exclusively in striated muscle. In mice, the absence of Ozz results in overt maturation defects of the sarcomeric apparatus. We identified beta-catenin as one of the target substrates of the Ozz-E3 in vivo. In the differentiating myofibers, Ozz-E3 regulates the levels of sarcolemma-associated beta-catenin by mediating its degradation via the proteasome. Expression of beta-catenin mutants that reduce the binding of Ozz to endogenous beta-catenin leads to Mb-beta-catenin accumulation and myofibrillogenesis defects similar to those observed in Ozz null myocytes. These findings reveal a novel mechanism of regulation of Mb-beta-catenin and the role of this pool of the protein in myofibrillogenesis, and implicate the Ozz-E3 ligase in the process of myofiber differentiation.
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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/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Catnb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epoxy Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/MYOG protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Myog protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Myogenin,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tenascin,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/cathestatin A
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1534-5807
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pubmed:author |
pubmed-author:BongiovanniAntonellaA,
pubmed-author:BostromJakeJ,
pubmed-author:CamposYvanY,
pubmed-author:ConawayJoan WelikyJW,
pubmed-author:D'AzzoAlessandraA,
pubmed-author:HahnChristopherC,
pubmed-author:HarrisA JohnAJ,
pubmed-author:MannLindaL,
pubmed-author:NastasiTommasoT,
pubmed-author:RottierRobbertR,
pubmed-author:ToyJames NJN
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
269-82
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:14960280-Aging,
pubmed-meshheading:14960280-Animals,
pubmed-meshheading:14960280-Blotting, Northern,
pubmed-meshheading:14960280-Blotting, Western,
pubmed-meshheading:14960280-Cells, Cultured,
pubmed-meshheading:14960280-Cytoskeletal Proteins,
pubmed-meshheading:14960280-Embryo, Mammalian,
pubmed-meshheading:14960280-Epoxy Compounds,
pubmed-meshheading:14960280-Gene Expression Regulation, Developmental,
pubmed-meshheading:14960280-Heart,
pubmed-meshheading:14960280-Humans,
pubmed-meshheading:14960280-Immunohistochemistry,
pubmed-meshheading:14960280-Mice,
pubmed-meshheading:14960280-Mice, Knockout,
pubmed-meshheading:14960280-Microscopy, Electron,
pubmed-meshheading:14960280-Muscle, Skeletal,
pubmed-meshheading:14960280-Muscle Development,
pubmed-meshheading:14960280-Mutation,
pubmed-meshheading:14960280-Myoblasts,
pubmed-meshheading:14960280-Myogenin,
pubmed-meshheading:14960280-Phenylalanine,
pubmed-meshheading:14960280-Precipitin Tests,
pubmed-meshheading:14960280-Repressor Proteins,
pubmed-meshheading:14960280-Sarcomeres,
pubmed-meshheading:14960280-Staining and Labeling,
pubmed-meshheading:14960280-Subcellular Fractions,
pubmed-meshheading:14960280-Tenascin,
pubmed-meshheading:14960280-Trans-Activators,
pubmed-meshheading:14960280-Ubiquitin-Protein Ligases,
pubmed-meshheading:14960280-Ubiquitins,
pubmed-meshheading:14960280-beta Catenin
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pubmed:year |
2004
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pubmed:articleTitle |
Ozz-E3, a muscle-specific ubiquitin ligase, regulates beta-catenin degradation during myogenesis.
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pubmed:affiliation |
Department of Genetics and Tumor Cell Biology, St. Jude Children's Research Hospital, 332 North Lauderdale Street, Memphis, TN 38105, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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