As for mechanisms of action, ecydsteroids seem to be able to cause a rapid Ca2+ influx in myocytes which leads to phosphorylation of Akt and thus protein synthesis.  This effect occurs after 10s of incubation, and is inhibited by PI3K inhibitors like seen in other studies, but also GPRC and PLC inhibitors; and when the cells are depleted of intra-cellular calcium Akt does not get phosphoraylized, and binding free calcium with EGTA lowered protein synthesis from 16% to 8%.  Calcium per se can be an important mediator of Akt and protein synthesis  , and ecdysteroids seem to work vicariously through Ca2+ and Akt. 
The 19S regulatory particle is responsible for stimulating the 20S to degrade proteins. A primary function of the 19S regulatory ATPases is to open the gate in the 20S that blocks the entry of substrates into the degradation chamber.  The mechanism by which the proteasomal ATPase open this gate has been recently elucidated.  20S gate opening, and thus substrate degradation, requires the C-termini of the proteasomal ATPases, which contains a specific motif (., HbYX motif). The ATPases C-termini bind into pockets in the top of the 20S, and tether the ATPase complex to the 20S proteolytic complex, thus joining the substrate unfolding equipment with the 20S degradation machinery. Binding of these C-termini into these 20S pockets by themselves stimulates opening of the gate in the 20S in much the same way that a "key-in-a-lock" opens a door.  The precise mechanism by which this "key-in-a-lock" mechanism functions has been structurally elucidated.