Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophy
Key result
Trim32 downregulation reduces fasting fiber atrophy and thin filament loss by preventing phosphorylated desmin degradation.
Population
Preclinical model of fasting-induced muscle atrophy
Comparison
Down-regulation of Trim32 or overexpression of… vs Control (normal Trim32 levels during fasting)
Design
Preclinical
Authors
Discussion
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Implication
Hypothesis-generating for Trim32 modulation in muscle atrophy; validation in human models required before clinical consideration.
Structured PICO
P
Population
Preclinical model of fasting-induced muscle atrophy
I
Intervention
Down-regulation of Trim32 or overexpression of an inhibitor of desmin polymerization
C
Comparator
Control (normal Trim32 levels during fasting)
O
Outcome
Degradation of thin filament (actin, tropomyosin, troponins) and Z-band (α-actinin) components, and desmin filamentssurrogate
Trim32-mediated ubiquitylation of phosphorylated desmin facilitates the breakdown of Z-bands and thin filaments during fasting-induced muscle atrophy.
Cite This Study
Cohen et al. (2012) studied Muscle atrophy. Down-regulation of Trim32 was evaluated on Degradation of thin filament and Z-band components. Down-regulation of Trim32 during fasting reduced fiber atrophy and the rapid loss of thin filaments by preventing the ubiquitylation and degradation of phosphorylated desmin.