The molecular mechanism underling blockage of muscle proteolysis by bee products in sarcopenic rodents involves an interplay of various signaling pathways. Royal jelly and bee pollen activated mTOR and its substrate AKT, which are suggested to inhibit muscular proteolysis [36,96]. Similar to the effect of royal jelly on catabolic genes in HET mice, treating both L6 myoblasts and rats with propolis, CAPE, and kaempferide resulted in potent activation of AKT in a PI3K-dependent manner [111], in addition to phosphorylation of IR, PI3K, and AMPK [70]. AKT, a key substrate of mTORC2, is a conserved serine/threonine nutrient sensing protein kinase that belongs to the PI3k-related protein kinase family. Upon presence of growth factors, PI3k gets activated by IR substrate resulting in stimulation of a series of signaling cascades that involve activation of AKT, which leads to further activation of mTORC1. mTORC1 activates the phosphorylation of two main regulators of cap-dependent protein synthesis: S6K and eIF4E [2,140]. In addition, mTORC1 contributes to autophagy—a turnover process that involves clearance of dysfunctional organelles and long-lived protein aggregations with provision of energy and macromolecular precursors in return—by binding with AMPK resulting in phosphorylation of autophagy genes such as Unc51-like kinase 1 at different sites [140]. In fact, royal jelly is reported to fine-tune the transcriptional activity of the FOXO through modulating the activity of insulin/IGF-1 signaling [141]. FOXO plays a major role in the activation of AKT pathway, which implicates regulation of multiple stress–response pathways such as ROS detoxification and DNA repair and translation. In addition, the FOXOs family exerts a direct effect on certain muscle atrophy genes such as MUSA1 and a formerly uncharacterized ligase known as Specific of Muscle Atrophy and Regulated by Transcription (SMART) [142].