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• W2278336600 abstract "We recently described a novel mechanism mediated by thick filament stress that controls load-dependent recruitment of myosin motors during muscle contraction (Linari et al. Nature in press). Here we show by time-resolved X-ray diffraction with a 5-m camera at beamline ID02 (ESRF) that this mechanism is also present in resting muscle. Force steps of 0.25 times the maximum active isometric force were imposed on resting mouse EDL muscles. Sarcomere length (SL), measured by X-ray diffraction with a 30-m camera, increased from SL 2.4 to 2.9 µm during the force step, and the intensities of the M2, M4 and M5 reflections associated with axial perturbations of myosin motors in the filament region containing myosin binding protein-C (MyBP-C) decreased by ca. 60%. These changes are linked to SL rather than filament stress, because similar reductions were produced by slowly increasing SL to 2.9 µm at low resting force. The spacing and fine structure of the M3 reflection were almost constant during the force step, but its intensity (IM3) decreased by ca. 50%, as did that of the first myosin layer line (IML1), indicating loss of the helical arrangement of the myosin motors associated with the thick filament OFF state. The spacing of the M6 reflection (SM6) increased by 0.4% during the step, indicating increased strain in the thick filament backbone. Much smaller changes in IM3, IML1 and SM6 were observed when SL was increased slowly from 2.4 to 2.9 µm at low force. Thus thick filament stress directly triggers the rapid release of myosin motors from the helical OFF-state in the absence of calcium, but MyBP-C links between the filaments do not mediate the effect. Supported by MIUR-PRIN and FIRB-Futuro in Ricerca (Italy), MRC (UK)." @default.
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• W2278336600 date "2016-02-01" @default.
• W2278336600 modified "2023-09-28" @default.
• W2278336600 title "Stress-Sensing Mobilizes Myosin Motors in the Thick Filaments of Resting Muscle" @default.
• W2278336600 doi "https://doi.org/10.1016/j.bpj.2015.11.131" @default.
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