title: Myosin rod phosphorylation and the catch state of molluscan muscles.
abstract: "Catch" is a prolonged state of tension in molluscan smooth muscles shown by mechanical measurements to be associated with the level of protein phosphorylation. Myosin isolated from these muscles is unusual in being phosphorylated in the rod portion by an endogenous kinase, like certain nonmuscle myosins. These findings suggest that the myosin rod is a target for phosphorylation and that this reaction may control the transition from catch to relaxation.
mesh_terms: D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000494:pharmacology; D000818:Animals; D049872:Bivalvia / Q000502:physiology*; D002118:Calcium / Q000502:physiology*; D000242:Cyclic AMP / Q000502:physiology; D004533:Egtazic Acid / Q000494:pharmacology; D066298:In Vitro Techniques; D009119:Muscle Contraction; D009218:Myosins / Q000378:metabolism / Q000502:physiology*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000502:physiology; D012969:Sodium Fluoride / Q000494:pharmacology
chemical_list: C022571:adenosine 5'-O-(3-thiotriphosphate); D004533:Egtazic Acid; D000255:Adenosine Triphosphate; D012969:Sodium Fluoride; D000242:Cyclic AMP; D011494:Protein Kinases; D010749:Phosphoprotein Phosphatases; D009218:Myosins; D002118:Calcium