Actin polymerization counteracts prewetting of N-WASP on supported lipid bilayers.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 39630867.
- Also identified by DOI 10.1073/pnas.2407497121 and PMC identifier 11648614.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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 <i>Caenorhabditis elegans</i> 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.
Medical subject headings
- Caenorhabditis elegans
- Wiskott-Aldrich Syndrome Protein, Neuronal
- Caenorhabditis elegans Proteins