Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions.

By Jie Du, Xiaonan H. Wang, Christiane Miereles, J. Bailey, R. Debigaré, Bin Zheng, S. Price, W. Mitch. Journal of Clinical Investigation, 2004

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Glucocorticoid-induced skeletal muscle atrophy. (2013, background): “Because the proteasome does not degrade intact myofibrils, it is thought that actin and myosin need to be dissociated from the myofibrils before they can be degraded by the UPS.”
The molecular basis of skeletal muscle atrophy. (2004, background): “It was also shown that diabetic rats and rats with cancer have increased muscle caspase activity (7, 18), and muscles of diabetic rats showed reduced proteolysis after treatment with a caspase-3 inhibitor (18).”
Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production (2008, background): “In the case of diabetes-induced muscle atrophy, it seems possible that caspase-3 is activated by caspase-12 (via a calcium release pathway) and/or activation of caspase-9 (via a mitochondrial pathway) (104).”
FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. (2007, background): “Evidence has been presented that caspases (Du et al., 2004) and/or calpains (Kramerova et al., 2005) might also play an essential role in enhancing muscle proteolysis during atrophy by promoting conversion of myoﬁbrillar proteins to forms easily digested by the ubiquitin-protea-some pathway.”