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

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Abstract

Cortical condensates, transient punctate-like structures rich in actin and the actin nucleation pathway member N-WASP, form during activation of the actin cortex in the C. elegans oocyte. Their emergence and spontaneous dissolution is linked to a phase separation process driven by chemical kinetics. However, the physical process that drives the onset of cortical condensate formation near membranes remains 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 new perspectives for understanding how the formation of complex intracellular structures is affected and controlled by phase separation.

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