The myosin-bound form of protein phosphatase 1 (PP-1M) is the enzyme that dephosphorylates native myosin in skeletal and cardiac muscles

The myosin-bound form of protein phosphatase 1 (PP-1_M) and the glycogen-bound form (PP-1_G) together account for virtually all the phosphatase activity in rabbit skeletal muscle extracts towards native myosin. PP-1_M has a 3-fold higher activity towards native myosin than does PP-1_G and accounts for at least 60% of the myosin phosphatase activity in rabbit skeletal muscle. PP-1_M accounts for 90% of the myosin phosphatase activity in bovine cardiac muscle, where PP-1_G is essentially absent. The high activity of PP-1_M towards native myosin appears to arise from interaction of the catalytic subunit with the putative myosin-binding subunit, since chymotryptic digestion liberates a catalytic subunit having the same characteristics as that released by limited proteolysis of PP-1_G. Protein phosphatase 2A in skeletal and cardiac muscles is very active towards the isolated myosin P-light chain, but ineffective in dephosphorylating native myosin. The results suggest that PP-1_M is the enzyme that dephosphorylates myosin in skeletal and cardiac muscle.