http://www.cnr.it/ontology/cnr/individuo/prodotto/ID12535
Ozz-E3 ubiquitin ligase targets sarcomeric embryonic myosin heavy chain during muscle development (Articolo in rivista)
- Type
- Label
- Ozz-E3 ubiquitin ligase targets sarcomeric embryonic myosin heavy chain during muscle development (Articolo in rivista) (literal)
- Anno
- 2010-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1371/journal.pone.0009866 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Campos Y1; Qiu X1; Zanoteli E1; Moshiach S1; Vergani N1; Bongiovanni A2; Harris AJ3; d'Azzo A1 (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0009866 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
- Mar 24;5(3):e9866. (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1 Department of Genetics and Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, United States of America, 2 Istituto di Biomedicina e di
Immunologia Molecolare, Consiglio Nazionale delle Ricerche, Palermo, Italy, 3 Department of Physiology, University of Otago Medical School, Dunedin, New Zealand (literal)
- Titolo
- Ozz-E3 ubiquitin ligase targets sarcomeric embryonic myosin heavy chain during muscle development (literal)
- Abstract
- Muscle contractile proteins are expressed as a series of developmental isoforms that are in constant dynamic remodeling during embryogenesis, but how obsolete molecules are recognized and removed is not known. Ozz is a developmentally regulated protein that functions as the adaptor component of a RING-type ubiquitin ligase complex specific to striated muscle. Ozz-/- mutants exhibit defects in myofibrillogenesis and myofiber differentiation. Here we show that Ozz targets the rod portion of embryonic myosin heavy chain and preferentially recognizes the sarcomeric rather than the soluble pool of myosin. We present evidence that Ozz binding to the embryonic myosin isoform within sarcomeric thick filaments marks it for ubiquitination and proteolytic degradation, allowing its replacement with neonatal or adult isoforms. This unique function positions Ozz within a system that facilitates sarcomeric myosin remodeling during muscle maturation and regeneration. Our findings identify Ozz-E3 as the ubiquitin ligase complex that interacts with and regulates myosin within its fully assembled cytoskeletal structure. (literal)
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