Loss of skeletal muscle mass or sarcopenia is the most common but understudied complication of alcoholic liver disease. Skeletal muscle proteolysis due to ethanol has not been systematically evaluated.A comprehensive approach was used to study the proteolytic pathways in muscle of patients with alcoholic cirrhosis and alcohol fed rodent along with in vitro studies in C2C12 myotubes exposed to 100mM ethanol for 24 hrs. Ubiquitin proteasome activity and autophagy were studied using immunoblots, real time PCR, proteasome activity, standard autophagy readouts including LC3 lipidation, p62 degradation and Beclin overexpression. C2C12 cells transfected with GFP‐LC3 and GFP‐mCherry‐LC3 reporter were also studied. Pulse chase experiments were performed with and without 3‐methyladenine. Immunoblots for components of the PI3K pathway‐Akt, mTOR, p70s6k and 4EBP activation, pAMPK as well as protein phosphatase 2A and PI3Kγ activity were quantified by thin layer chromatography. Ubiquitin proteasomal activity was unaltered and autophagy was increased in the myotubes and in vivo with ethanol. mTOR and its target protein phosphorylation was lower with ethanol exposure. Increased PP2A activity resulted in an AMPK independent mTOR dependent increase in autophagy.