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 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.
journal_name
Dev Celljournal_title
Developmental cellauthors
Nastasi T,Bongiovanni A,Campos Y,Mann L,Toy JN,Bostrom J,Rottier R,Hahn C,Conaway JW,Harris AJ,D'Azzo Adoi
10.1016/s1534-5807(04)00020-6keywords:
subject
Has Abstractpub_date
2004-02-01 00:00:00pages
269-82issue
2eissn
1534-5807issn
1878-1551pii
S1534-5807(04)00020-6journal_volume
6pub_type
杂志文章abstract：:To enable stratification and barrier function, the epidermis must permit self-renewal while maintaining adhesive connections. By generating K14-GFP-actin mice to monitor actin dynamics in cultured primary keratinocytes, we uncovered a role for the actin cytoskeleton in establishing cellular organization. During epider...
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