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Control of lipid domain organization by a biomimetic contractile actomyosin cortex.

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Vogel,  Sven Kenjiro
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Greiss,  Ferdinand
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Khmelinskaia,  Alena
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Schwille,  Petra
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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elife-24350-v2.pdf
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Citation

Vogel, S. K., Greiss, F., Khmelinskaia, A., & Schwille, P. (2017). Control of lipid domain organization by a biomimetic contractile actomyosin cortex. eLife, 6: e24350. doi:10.7554/eLife.24350.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-E216-F
Abstract
The cell membrane is a heterogeneously organized composite with lipid-protein micro-domains. The contractile actin cortex may govern the lateral organization of these domains in the cell membrane, yet the underlying mechanisms are not known. We recently reconstituted minimal actin cortices (MACs) (Vogel et al., 2013b) and here advanced our assay to investigate effects of rearranging actin filaments on the lateral membrane organization by introducing various phase-separated lipid mono- and bilayers to the MACs. The addition of actin filaments reorganized membrane domains. We found that the process reached a steady state where line tension and lateral crowding balanced. Moreover, the phase boundary allowed myosin driven actin filament rearrangements to actively move individual lipid domains, often accompanied by their shape change, fusion or splitting. Our findings illustrate how actin cortex remodeling in cells may control dynamic rearrangements of lipids and other molecules inside domains without directly binding to actin filaments.