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

Autor:	Wiegand T; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany.; Max Planck Institute for the Physics of Complex Systems, Dresden 01187, Germany., Liu J; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany.; Center for Systems Biology Dresden, Dresden 01307, Germany., Vogeley L; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany., LuValle-Burke I; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany.; Max Planck Institute for the Physics of Complex Systems, Dresden 01187, Germany., Geisler J; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany.; Max Planck School Matter to Life, Heidelberg 69120, Germany., Fritsch AW; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany.; Max Planck Institute for the Physics of Complex Systems, Dresden 01187, Germany., Hyman AA; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany.; Cluster of Excellence Physics of Life, Technische Universität Dresden, Dresden 01307, Germany., Grill SW; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany.; Cluster of Excellence Physics of Life, Technische Universität Dresden, Dresden 01307, Germany.
Jazyk:	angličtina
Zdroj:	Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Dec 10; Vol. 121 (50), pp. e2407497121. Date of Electronic Publication: 2024 Dec 04.
DOI:	10.1073/pnas.2407497121
Abstrakt:	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. Competing Interests: Competing interests statement:A.A.H. is cofounder and member of the scientific advisory board of Dewpoint Therapeutics Inc.
Databáze:	MEDLINE
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