Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophy

During muscle atrophy, myofibrillar proteins are degraded in an ordered process in which MuRF1 catalyzes ubiquitylation of thick filament components (Cohen et al. 2009. J. Cell Biol. http://dx.doi.org/10.1083/jcb.200901052). Here, we show that another ubiquitin ligase, Trim32, ubiquitylates thin fil...

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Detalles Bibliográficos
Autores principales: Cohen, Shenhav, Zhai, Bo, Gygi, Steven P., Goldberg, Alfred L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2012
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3514026/
https://www.ncbi.nlm.nih.gov/pubmed/22908310
http://dx.doi.org/10.1083/jcb.201110067

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3514026/
https://www.ncbi.nlm.nih.gov/pubmed/22908310
http://dx.doi.org/10.1083/jcb.201110067

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