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Beating Vesicles: Encapsulated Protein Oscillations Cause Dynamic Membrane Deformations.

Thomas Litschel1, Beatrice Ramm1, Roel Maas1

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The bacterial Min protein system, when encapsulated in giant unilamellar vesicles (GUVs), drives dynamic shape changes and even autonomous division. This self-organization demonstrates how protein patterns can mechanically alter membrane compartments.

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Area of Science:

  • Biophysics
  • Cell Biology
  • Biochemistry

Background:

  • The bacterial Min protein system regulates cell division through self-organization.
  • Giant unilamellar vesicles (GUVs) are model systems for studying cellular processes.
  • Understanding protein self-organization and its mechanical effects on membranes is crucial.

Purpose of the Study:

  • To investigate the spatiotemporal patterns of the bacterial Min protein system within GUVs.
  • To explore the relationship between Min protein dynamics and GUV mechanical properties.
  • To demonstrate how protein self-organization can induce autonomous membrane shape changes and division.

Main Methods:

  • Encapsulation of the bacterial Min protein system in GUVs.
  • Confocal fluorescence microscopy to observe protein patterns and vesicle dynamics.
  • Analysis of vesicle shape changes and mechanical properties.

Main Results:

  • Observed distinct spatiotemporal patterns of Min proteins inside GUVs.
  • Demonstrated active changes in GUV shape synchronized with Min protein oscillations.
  • Documented two modes of oscillating shape changes: fission-fusion and budding-merging.
  • Showcased Min protein relocation affecting lipid bilayer mechanical properties.

Conclusions:

  • Reaction-diffusion-based protein self-organization can directly cause visible mechanical effects on membrane compartments.
  • The Min system can drive autonomous vesicle division without cytoskeletal involvement.
  • This study links molecular self-organization to macroscopic mechanical phenomena in model cell compartments.