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Controlled division of cell-sized vesicles by low densities of membrane-bound proteins

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Steinkühler,  Jan
Rumiana Dimova, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Knorr,  Roland L.
Roland Knorr, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Zhao,  Ziliang
Rumiana Dimova, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Bhatia,  Tripta
Rumiana Dimova, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Dimova,  Rumiana
Rumiana Dimova, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Lipowsky,  Reinhard
Reinhard Lipowsky, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

Steinkühler, J., Knorr, R. L., Zhao, Z., Bhatia, T., Bartelt, S. M., Wegner, S., et al. (2020). Controlled division of cell-sized vesicles by low densities of membrane-bound proteins. Nature Communications, 11: 905. doi:10.1038/s41467-020-14696-0.


Cite as: https://hdl.handle.net/21.11116/0000-0005-8D59-9
Abstract
The proliferation of life on earth is based on the ability of single cells to divide into two daughter cells. During cell division, the plasma membrane undergoes a series of morphological transformations which ultimately lead to membrane fission. Here, we show that analogous remodeling processes can be induced by low densities of proteins bound to the membranes of cell-sized lipid vesicles. Using His-tagged fluorescent proteins, we are able to precisely control the spontaneous curvature of the vesicle membranes. By fine-tuning this curvature, we obtain dumbbell-shaped vesicles with closed membrane necks as well as neck fission and complete vesicle division. Our results demonstrate that the spontaneous curvature generates constriction forces around the membrane necks and that these forces can easily cover the force range found in vivo. Our approach involves only one species of membrane-bound proteins at low densities, thereby providing a simple and extendible module for bottom-up synthetic biology.