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F-actin architecture determines constraints on myosin thick filament motion

Author

Listed:
  • Camelia G. Muresan

    (Yale University
    Yale University)

  • Zachary Gao Sun

    (Yale University
    Yale University)

  • Vikrant Yadav

    (Yale University
    Yale University)

  • A. Pasha Tabatabai

    (Yale University
    Yale University)

  • Laura Lanier

    (Yale University
    Yale University)

  • June Hyung Kim

    (Purdue University)

  • Taeyoon Kim

    (Purdue University)

  • Michael P. Murrell

    (Yale University
    Yale University
    Yale University)

Abstract

Active stresses are generated and transmitted throughout diverse F-actin architectures within the cell cytoskeleton, and drive essential behaviors of the cell, from cell division to migration. However, while the impact of F-actin architecture on the transmission of stress is well studied, the role of architecture on the ab initio generation of stresses remains less understood. Here, we assemble F-actin networks in vitro, whose architectures are varied from branched to bundled through F-actin nucleation via Arp2/3 and the formin mDia1. Within these architectures, we track the motions of embedded myosin thick filaments and connect them to the extent of F-actin network deformation. While mDia1-nucleated networks facilitate the accumulation of stress and drive contractility through enhanced actomyosin sliding, branched networks prevent stress accumulation through the inhibited processivity of thick filaments. The reduction in processivity is due to a decrease in translational and rotational motions constrained by the local density and geometry of F-actin.

Suggested Citation

  • Camelia G. Muresan & Zachary Gao Sun & Vikrant Yadav & A. Pasha Tabatabai & Laura Lanier & June Hyung Kim & Taeyoon Kim & Michael P. Murrell, 2022. "F-actin architecture determines constraints on myosin thick filament motion," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34715-6
    DOI: 10.1038/s41467-022-34715-6
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    References listed on IDEAS

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    1. M. Fritzsche & D. Li & H. Colin-York & V. T. Chang & E. Moeendarbary & J. H. Felce & E. Sezgin & G. Charras & E. Betzig & C. Eggeling, 2017. "Self-organizing actin patterns shape membrane architecture but not cell mechanics," Nature Communications, Nature, vol. 8(1), pages 1-14, April.
    2. A. Chaigne & C. Campillo & N. S. Gov & R. Voituriez & C. Sykes & M. H. Verlhac & M. E. Terret, 2015. "A narrow window of cortical tension guides asymmetric spindle positioning in the mouse oocyte," Nature Communications, Nature, vol. 6(1), pages 1-10, May.
    3. Daniel S. Seara & Vikrant Yadav & Ian Linsmeier & A. Pasha Tabatabai & Patrick W. Oakes & S. M. Ali Tabei & Shiladitya Banerjee & Michael P. Murrell, 2018. "Entropy production rate is maximized in non-contractile actomyosin," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
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    Cited by:

    1. Ryota Sakamoto & Michael P. Murrell, 2024. "F-actin architecture determines the conversion of chemical energy into mechanical work," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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