Phase separated VASP droplets modulate actin filament assembly and dynamics

Actin is a major component of the cytoskeleton that plays a critical role in maintaining cell shape, driving cell migration, and supporting cell division. Actin assembles into diverse network architectures through the coordinated action of numerous actin-binding proteins (ABPs), some of which can undergo liquid–liquid phase separation (LLPS). Despite increasing evidence of LLPS in the actin cytoskeleton, our understanding of how these condensates influence the formation of higher-order actin structures remains limited. For example, at the leading edge of migrating cells, clusters of vasodilator-stimulated phosphoprotein (VASP) have been implicated in the formation of filopodia, exploratory finger-like protrusive structure, but the precise functional role of clusters remains unclear. In this talk, I will present our experimental results on how phase-separated VASP condensates interact with actin filaments, modulate their assembly dynamics, and give rise to diverse network organizations.