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Entropy production rate is maximized in non-contractile actomyosin

Author

Listed:
  • Daniel S. Seara

    (Yale University
    Systems Biology Institute, Yale University)

  • Vikrant Yadav

    (Systems Biology Institute, Yale University
    Yale University)

  • Ian Linsmeier

    (Systems Biology Institute, Yale University
    Yale University)

  • A. Pasha Tabatabai

    (Systems Biology Institute, Yale University
    Yale University)

  • Patrick W. Oakes

    (University of Rochester)

  • S. M. Ali Tabei

    (University of Northern Iowa)

  • Shiladitya Banerjee

    (Institute for the Physics of Living Systems, University College London)

  • Michael P. Murrell

    (Yale University
    Systems Biology Institute, Yale University
    Yale University)

Abstract

The actin cytoskeleton is an active semi-flexible polymer network whose non-equilibrium properties coordinate both stable and contractile behaviors to maintain or change cell shape. While myosin motors drive the actin cytoskeleton out-of-equilibrium, the role of myosin-driven active stresses in the accumulation and dissipation of mechanical energy is unclear. To investigate this, we synthesize an actomyosin material in vitro whose active stress content can tune the network from stable to contractile. Each increment in activity determines a characteristic spectrum of actin filament fluctuations which is used to calculate the total mechanical work and the production of entropy in the material. We find that the balance of work and entropy does not increase monotonically and the entropy production rate is maximized in the non-contractile, stable state of actomyosin. Our study provides evidence that the origins of entropy production and activity-dependent dissipation relate to disorder in the molecular interactions between actin and myosin.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07413-5
    DOI: 10.1038/s41467-018-07413-5
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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.
    2. 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.
    3. Agustin D. Pizarro & Claudio L. A. Berli & Galo J. A. A. Soler-Illia & Martín G. Bellino, 2022. "Droplets in underlying chemical communication recreate cell interaction behaviors," Nature Communications, Nature, vol. 13(1), pages 1-10, December.

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