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Mechanisms of protein synthesis activation following exercise: new pieces to the increasingly complex puzzle

Exercise promotes muscle adaptation by modulating gene expression and protein synthesis. The current knowledge states that the acute increase in the rate of protein synthesis following muscle contractions is controlled by the mammalian target of rapamycin complex 1 (mTORC1). Although nutritional state and protein provision tailor the response following exercise, muscle contraction is believed to promote mTORC1 activation per se in a mechanical and/or stress related fashion via an Akt‐independent mechanism. Few candidates appear recurrently in the literature as the mTORC1 activator. Phosphatidic acid synthetized from diacylglycerol from muscle membranes and its direct binding to mTOR is one of the most prominent candidates. Protein kinases associated with the sarcomere, such as focal adhesion kinases (FAK), are also believed to potentially mediate mechanical signalling towards mTORC1. Additionally, the extracellular signal‐regulated kinase (ERK) pathway cross‐talks at many levels with the tuberous sclerosis 1/2 proteins (TSC1/2)‐mTORC1‐70 kDa ribosomal protein S6 kinase 1 (p70S6K1) axis and thus can also be partially responsible for this activation (Fig. 1). Instead of a single master modulator of protein synthesis, it is likely that this key cellular process is regulated at multiple levels by intrinsic feedback, synergistic and alternative mechanisms that may be more or less predominant depending on the stimulus and the nutritional/physiological status of the cell.