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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...
Wedi'i Gadw mewn:
| Prif Awduron: | , , , |
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| Fformat: | Artigo |
| Iaith: | Inglês |
| Cyhoeddwyd: |
The Rockefeller University Press
2012
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| Pynciau: | |
| Mynediad Ar-lein: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3514026/ https://ncbi.nlm.nih.gov/pubmed/22908310 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1083/jcb.201110067 |
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