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

@inproceedings{Cohen2012UbiquitylationBT,
  title={Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and
thin filaments in muscle atrophy},
  author={Shenhav Cohen and Bo Zhai and Steven P Gygi and Alfred L Goldberg},
  booktitle={The Journal of cell biology},
  year={2012}
}
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 filament (actin, tropomyosin, troponins) and Z-band (α-actinin) components and promotes their degradation. Down-regulation of Trim32 during fasting reduced fiber atrophy and the rapid loss of thin… CONTINUE READING
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