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Self-organizing actin patterns shape membrane architecture but not cell mechanics

Author

Listed:
  • M. Fritzsche

    (MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford)

  • D. Li

    (National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

  • H. Colin-York

    (MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford)

  • V. T. Chang

    (MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford
    Wellcome Trust Centre for Human Genetics, University of Oxford)

  • E. Moeendarbary

    (Massachusetts Institute of Technology
    University College London)

  • J. H. Felce

    (MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford)

  • E. Sezgin

    (MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford)

  • G. Charras

    (University College London)

  • E. Betzig

    (Howard Hughes Medical Institute, Janelia Research Campus)

  • C. Eggeling

    (MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford)

Abstract

Cell-free studies have demonstrated how collective action of actin-associated proteins can organize actin filaments into dynamic patterns, such as vortices, asters and stars. Using complementary microscopic techniques, we here show evidence of such self-organization of the actin cortex in living HeLa cells. During cell adhesion, an active multistage process naturally leads to pattern transitions from actin vortices over stars into asters. This process is primarily driven by Arp2/3 complex nucleation, but not by myosin motors, which is in contrast to what has been theoretically predicted and observed in vitro. Concomitant measurements of mechanics and plasma membrane fluidity demonstrate that changes in actin patterning alter membrane architecture but occur functionally independent of macroscopic cortex elasticity. Consequently, tuning the activity of the Arp2/3 complex to alter filament assembly may thus be a mechanism allowing cells to adjust their membrane architecture without affecting their macroscopic mechanical properties.

Suggested Citation

  • 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.
  • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14347
    DOI: 10.1038/ncomms14347
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    Cited by:

    1. Haoqing Jerry Wang & Yao Wang & Seyed Sajad Mirjavadi & Tomas Andersen & Laura Moldovan & Parham Vatankhah & Blake Russell & Jasmine Jin & Zijing Zhou & Qing Li & Charles D. Cox & Qian Peter Su & Lini, 2024. "Microscale geometrical modulation of PIEZO1 mediated mechanosensing through cytoskeletal redistribution," Nature Communications, Nature, vol. 15(1), pages 1-17, 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.

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