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Subunit exchange between smooth muscle myosin filaments.
1Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254.
The Journal of Cell Biology
|December 1, 1987
Summary
Smooth muscle myosin filaments are dynamic, readily exchanging components. MgATP disassembles dephosphorylated myosin, revealing a mechanism for filament disassembly.
Area of Science:
- Biochemistry
- Cell Biology
- Muscle Physiology
Background:
- Phosphorylated smooth muscle myosin forms stable filaments, while dephosphorylated myosin disassembles in MgATP.
- The dynamic behavior and copolymer stability of smooth muscle myosin filaments were previously unknown.
Purpose of the Study:
- To investigate the stability of copolymers of phosphorylated and dephosphorylated smooth muscle myosin.
- To elucidate the exchange dynamics of myosin molecules within filaments.
Main Methods:
- Gel filtration, sedimentation velocity, and pelleting assays were employed to analyze filament composition.
- Electron microscopy with gold-labeled probes was used to visualize molecular exchange between filaments.
Main Results:
- MgATP dissociated dephosphorylated myosin from copolymers, regardless of other components.
- Myosin molecules were shown to rapidly and extensively exchange between filaments, indicating dynamic structures.
- Filament composition changes in response to solvent conditions, with MgATP promoting disassembly via folded monomers.
Conclusions:
- Smooth muscle myosin filaments are dynamic structures capable of altering composition.
- MgATP-induced disassembly occurs through the dissociation of dephosphorylated myosin, likely via a monomeric pool.