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Actin polymerization counteracts prewetting of N-WASP on supported lipid bilayers.

MPS-Authors
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Wiegand,  Tina
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Vogeley,  Lutz
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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LuValle-Burke,  Isabel
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Fritsch,  Anatol
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Hyman,  Anthony
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Grill,  Stephan W.
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Wiegand, T., Liu, J., Vogeley, L., LuValle-Burke, I., Geisler, J., Fritsch, A., et al. (2024). Actin polymerization counteracts prewetting of N-WASP on supported lipid bilayers. Proceedings of the National Academy of Sciences of the United States of America, 121(50): e2407497121. doi:10.1073/pnas.2407497121.


Cite as: https://hdl.handle.net/21.11116/0000-0010-D4E5-C
Abstract
Cortical condensates, transient punctate-like structures rich in actin and the actin nucleation pathway member Neural Wiskott-Aldrich syndrome protein (N-WASP), form during activation of the actin cortex in the Caenorhabditis elegans oocyte. Their emergence and spontaneous dissolution is linked to a phase separation process driven by chemical kinetics. However, the mechanisms that drive the onset of cortical condensate formation near membranes remain unexplored. Here, using a reconstituted phase separation assay of cortical condensate proteins, we demonstrate that the key component, N-WASP, can collectively undergo surface condensation on supported lipid bilayers via a prewetting transition. Actin partitions into the condensates, where it polymerizes and counteracts the N-WASP prewetting transition. Taken together, the dynamics of condensate-assisted cortex formation appear to be controlled by a balance between surface-assisted condensate formation and polymer-driven condensate dissolution. This opens perspectives for understanding how the formation of complex intracellular structures is affected and controlled by phase separation.