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Force generation by skeletal muscle is controlled by mechanosensing in myosin filaments

机译：骨骼肌产生的力由肌球蛋白丝中的机械传感控制

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摘要

Contraction of both skeletal muscle and the heart is thought to be controlled by a calcium-dependent structural change in the actin-containing thin filaments, which permits the binding of myosin motors from the neighbouring thick filaments to drive filament sliding(1-3). Here we show by synchrotron small-angle X-ray diffraction of frog (Rana temporaria) single skeletal muscle cells that, although the well-known thin-filament mechanism is sufficient for regulation of muscle shortening against low load, force generation against high load requires a second permissive step linked to a change in the structure of the thick filament. The resting (switched 'OFF') structure of the thick filament is characterized by helical tracks of myosin motors on the filament surface and a short backbone periodicity(2,4,5). This OFF structure is almost completely preserved during low-load shortening, which is driven by a small fraction of constitutively active (switched 'ON') myosin motors outside thick-filament control. At higher load, these motors generate sufficient thick-filament stress to trigger the transition to its long-periodicity ON structure, unlocking the major population of motors required for high-load contraction. This concept of the thick filament as a regulatory mechanosensor provides a novel explanation for the dynamic and energetic properties of skeletal muscle. A similar mechanism probably operates in the heart.
机译：骨骼肌和心脏的收缩被认为是由含肌动蛋白的细丝中钙相关的结构变化所控制的，它允许肌球蛋白马达与相邻粗丝的结合从而驱动细丝滑动（1-3）。在这里，我们通过同步加速器小角度X射线衍射显示了青蛙（Rana temporaria）单个骨骼肌细胞，尽管众所周知的细丝机制足以调节针对低负荷的肌肉缩短，但需要针对高负荷的力产生第二个允许步骤与粗丝结构的变化有关。粗细丝的静止（切换为``关闭''）结构的特征是细丝表面上肌球蛋白马达的螺旋轨迹和较短的骨架周期性（2,4,5）。在低负载起酥油期间，这种OFF结构几乎完全得以保留，这是由一小部分厚丝控制之外的本构主动（接通“ ON”）肌球蛋白电动机驱动的。在更高的负载下，这些电机会产生足够的厚丝应力，从而触发向其长周期ON结构的过渡，从而释放出高负载收缩所需的大量电机。粗细丝作为调节型机械传感器的概念为骨骼肌的动态和能量特性提供了新颖的解释。类似的机制可能在心脏中起作用。

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  • 来源
    《Nature》 |2015年第7581期|276-279|共4页
  • 作者

    Linari Marco; Brunello Elisabetta; Reconditi Massimo; Fusi Luca; Caremani Marco; Narayanan Theyencheri; Piazzesi Gabriella; Lombardi Vincenzo; Irving Malcolm;

  • 作者单位

    Univ Florence, Dept Biol, Physiol Lab, I-50019 Florence, Italy|UdR Firenze, Consorzio Nazl Interuniv Sci Fis Mat, I-50019 Florence, Italy;

    Univ Florence, Dept Biol, Physiol Lab, I-50019 Florence, Italy;

    Univ Florence, Dept Biol, Physiol Lab, I-50019 Florence, Italy|UdR Firenze, Consorzio Nazl Interuniv Sci Fis Mat, I-50019 Florence, Italy;

    Kings Coll London, Randall Div, London SE1 1UL, England|Kings Coll London, BHF Ctr Res Excellence, London SE1 1UL, England;

    Univ Florence, Dept Biol, Physiol Lab, I-50019 Florence, Italy;

    European Synchrotron Radiat Facil, F-38043 Grenoble, France;

    Univ Florence, Dept Biol, Physiol Lab, I-50019 Florence, Italy;

    Univ Florence, Dept Biol, Physiol Lab, I-50019 Florence, Italy;

    Kings Coll London, Randall Div, London SE1 1UL, England|Kings Coll London, BHF Ctr Res Excellence, London SE1 1UL, England;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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