Abstract
The assembly of myosin-II into filaments is required for cytokinesis, cell motility, and the maintenance of cell morphology. Myosin-II filament dynamics are under strict spatial and temporal control; however, the molecular mechanisms modulating assembly and disassembly are poorly understood. Our studies focus on the contribution of the C-terminal coiled-coil and the nonhelical tailpiece to the regulation of myosin-IIA filament assembly. We probed the intrinsic dynamics of the coiled-coil and its interaction with S100A4, a major metastasis factor. Using sedimentation equilibrium, hydrogen-deuterium exchange, and thermal melt CD spectroscopy, we showed that C-terminal coiled-coil of the myosin-IIA heavy chain exhibits significant conformational plasticity. We propose a mechanism in which S100A4 binding to the C-terminal coiled-coil locally unzips the two polypeptide chains of the dimeric myosin-IIA coiled-coil, and thus modulates myosin-IIA filament assembly. We are testing this hypothesis by using electron spin resonance (EPR) spectroscopy to monitor conformational changes in the myosin-IIA coiled-coil upon S100A4 binding.
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