title: Effects of light chain phosphorylation and skeletal myosin on the stability of non-muscle myosin filaments.
abstract: The effect of light chain phosphorylation and the presence of skeletal muscle myosin on the stability of non-phosphorylated non-muscle myosin filaments was investigated. Purified skeletal, brush border and thymus myosins were assembled in vitro into hybrid filaments consisting of varying proportions of (1) non-muscle and skeletal myosins, or (2) phosphorylated and non-phosphorylated non-muscle myosins. The stability of these hetero- and homopolymers in the presence of MgATP was determined using sedimentation, gel electrophoresis and immunochemical techniques. In addition, the effect of a monoclonal antibody, binding to the tip of brush border myosin tail, on the assembly of the homo- and heteropolymers, was tested. Filamentous non-phosphorylated non-muscle myosin was disassembled by MgATP to the same extent whether in homo- or heteropolymers, indicating that skeletal myosin has no stabilising effect on the hybrid filaments. The presence of small amounts of phosphorylated non-muscle myosin was, however, found to prevent the complete disassembly by MgATP of non-phosphorylated non-muscle myosin filaments, indicating that light chain phosphorylation stabilizes co-operatively non-muscle myosin filaments. The monoclonal antibody prevented the assembly of brush border myosin into both homo- and heteropolymers, and its effect on the filaments was compared with that of MgATP.
mesh_terms: D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D000911:Antibodies, Monoclonal; D004591:Electrophoresis, Polyacrylamide Gel; D008854:Microscopy, Electron; D008871:Microvilli / Q000032:analysis; D009132:Muscles / Q000032:analysis; D009218:Myosins / Q000378:metabolism*; D010766:Phosphorylation; D011108:Polymers; D013950:Thymus Gland; D014461:Ultracentrifugation
chemical_list: D000911:Antibodies, Monoclonal; D011108:Polymers; D000255:Adenosine Triphosphate; D009218:Myosins