http://www.cnr.it/ontology/cnr/individuo/prodotto/ID12193
Ozz-E3, A Muscle-Specific Ubiquitin Ligase, Regulates b-Catenin Degradation during Myogenesis (Articolo in rivista)
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- Ozz-E3, A Muscle-Specific Ubiquitin Ligase, Regulates b-Catenin Degradation during Myogenesis (Articolo in rivista) (literal)
- Anno
- 2004-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/S1534-5807(04)00020-6 (literal)
- Alternative label
Tommaso Nastasi,1,4; Antonella Bongiovanni,1,4,5; Yvan Campos,1; Linda Mann,1; James N. Toy,1;
Jake Bostrom,1; Robbert Rottier,1,6; Christopher Hahn,1,7; Joan Weliky Conaway,2; A. John Harris,3 and Alessandra d'Azzo1,* (2004)
Ozz-E3, A Muscle-Specific Ubiquitin Ligase, Regulates b-Catenin Degradation during Myogenesis
in Developmental cell; Cell Press, Cambridge (Stati Uniti d'America)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Tommaso Nastasi,1,4; Antonella Bongiovanni,1,4,5; Yvan Campos,1; Linda Mann,1; James N. Toy,1;
Jake Bostrom,1; Robbert Rottier,1,6; Christopher Hahn,1,7; Joan Weliky Conaway,2; A. John Harris,3 and Alessandra d'Azzo1,* (literal)
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- http://www.sciencedirect.com/science/article/pii/S1534580704000206 (literal)
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- 1Department of Genetics and Tumor Cell Biology St. Jude Children's Research Hospital 332 North Lauderdale Street Memphis, Tennessee 38105; 2Stowers Institute for Medical Research 1000 East 50th Street Kansas City, Missouri 64110; 3Developmental Biology Unit and Department of Physiology University of Otago Dunedin New Zealand
*Correspondence: alessandra.dazzo@stjude.org; 4These authors contributed equally to this work; 5Present address: Istituto di Biomedicina e Immunologia Molecolare, IBIM Consiglio Nazionale delle Ricerche, Palermo, Italy; 6Present address: MGC-Department of Cell Biology, The Erasmus University, Rotterdam, Netherlands. 7Present
address: Vascular Biology Laboratory, Hanson Center for Cancer Research, Adelaide, Australia. (literal)
- Titolo
- Ozz-E3, A Muscle-Specific Ubiquitin Ligase, Regulates b-Catenin Degradation during Myogenesis (literal)
- Abstract
- 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 b-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 b-catenin by mediating its degradation via the proteasome. Expression of b-catenin mutants that reduce the binding of Ozz to endogenous b-catenin leads to Mb-b-catenin accumulation and myofibrillogenesis defects similar to those observed in Ozz null myocytes. These findings reveal a novel mechanism of regulation of Mb-b-catenin and the role of this pool of the protein in myofibrillogenesis, and implicate the Ozz-E3 ligase in the process of myofiber differentiation. (literal)
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