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Reconstitution of contractile actomyosin rings in vesicles

Author

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  • Thomas Litschel

    (Department of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry)

  • Charlotte F. Kelley

    (Department of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry
    Department of Structural Cell Biology, Max Planck Institute of Biochemistry)

  • Danielle Holz

    (Lehigh University)

  • Maral Adeli Koudehi

    (Lehigh University)

  • Sven K. Vogel

    (Department of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry)

  • Laura Burbaum

    (Department of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry)

  • Naoko Mizuno

    (Department of Structural Cell Biology, Max Planck Institute of Biochemistry)

  • Dimitrios Vavylonis

    (Lehigh University)

  • Petra Schwille

    (Department of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry)

Abstract

One of the grand challenges of bottom-up synthetic biology is the development of minimal machineries for cell division. The mechanical transformation of large-scale compartments, such as Giant Unilamellar Vesicles (GUVs), requires the geometry-specific coordination of active elements, several orders of magnitude larger than the molecular scale. Of all cytoskeletal structures, large-scale actomyosin rings appear to be the most promising cellular elements to accomplish this task. Here, we have adopted advanced encapsulation methods to study bundled actin filaments in GUVs and compare our results with theoretical modeling. By changing few key parameters, actin polymerization can be differentiated to resemble various types of networks in living cells. Importantly, we find membrane binding to be crucial for the robust condensation into a single actin ring in spherical vesicles, as predicted by theoretical considerations. Upon force generation by ATP-driven myosin motors, these ring-like actin structures contract and locally constrict the vesicle, forming furrow-like deformations. On the other hand, cortex-like actin networks are shown to induce and stabilize deformations from spherical shapes.

Suggested Citation

  • Thomas Litschel & Charlotte F. Kelley & Danielle Holz & Maral Adeli Koudehi & Sven K. Vogel & Laura Burbaum & Naoko Mizuno & Dimitrios Vavylonis & Petra Schwille, 2021. "Reconstitution of contractile actomyosin rings in vesicles," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
  • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-22422-7
    DOI: 10.1038/s41467-021-22422-7
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    Cited by:

    1. Jorik Waeterschoot & Willemien Gosselé & Špela Lemež & Xavier Casadevall i Solvas, 2024. "Artificial cells for in vivo biomedical applications through red blood cell biomimicry," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Shunshi Kohyama & Adrián Merino-Salomón & Petra Schwille, 2022. "In vitro assembly, positioning and contraction of a division ring in minimal cells," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. Nishkantha Arulkumaran & Mervyn Singer & Stefan Howorka & Jonathan R. Burns, 2023. "Creating complex protocells and prototissues using simple DNA building blocks," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    4. Aravind Chandrasekaran & Kristin Graham & Jeanne C. Stachowiak & Padmini Rangamani, 2024. "Kinetic trapping organizes actin filaments within liquid-like protein droplets," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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