Effects of light chain phosphorylation and skeletal myosin on the stability of non-muscle myosin filaments
Journal of Molecular Biology, ISSN: 0022-2836, Vol: 198, Issue: 2, Page: 253-262
1987
- 15Citations
- 7Captures
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Metrics Details
- Citations15
- Citation Indexes15
- 15
- CrossRef11
- Captures7
- Readers7
Article Description
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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0022283687903111; http://dx.doi.org/10.1016/0022-2836(87)90311-1; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0023661108&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/3501477; https://linkinghub.elsevier.com/retrieve/pii/0022283687903111; http://dx.doi.org/10.1016/0022-2836%2887%2990311-1; https://dx.doi.org/10.1016/0022-2836%2887%2990311-1
Elsevier BV
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