Increased phosphorylation in vitro of a cytosolic polypeptide resolved from denervated skeletal muscle.
The in vitro phosphorylation of a 40,400-dalton, cytosolic polypeptide from the soleus muscle of the rat is increased twofold within 24 hr after cutting the motor nerve fibers to this muscle. This involves an ATP-phosphotransferase reaction which we have reported to be inhibited by a specific cyclic AMP-dependent protein kinase inhibitor. The phosphorylated polypeptide does not electrophoretically comigrate on SDS-polyacrylamide gels with the 38,000-dalton catalytic subunit of cyclic AMP-dependent protein kinase which is known to undergo a site-specific autophosphorylation in skeletal muscle.
D000818:Animals; D000242:Cyclic AMP / Q000494:pharmacology; D003600:Cytosol / Q000378:metabolism; D008297:Male; D008970:Molecular Weight; D009121:Muscle Denervation; D009132:Muscles / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats
D010455:Peptides; D000242:Cyclic AMP; D011494:Protein Kinases