A balance between nucleating and elongating actin filaments controls deformation of protein condensates.

ABSTRACT: Protein condensates use multivalent binding and surface tension to assemble actin filaments into diverse architectures, reminiscent of filopodia and stress fibers. During this process, nucleation of new filaments and elongation of existing filaments inherently compete for a shared pool of actin monomers. Here we show that a balance between these competing processes is required to deform condensates of VASP, an actin binding protein, into structures with high aspect ratios. Addition of magnesium, which promotes filament nucleation, helped actin to deform condensates into high aspect ratio structures. In contrast, addition of profilin, which inhibits filament nucleation, allowing existing filaments to elongate, caused actin to assemble into ring-like bundles that failed to substantially incr

SUBMITTER: Walker C 

PROVIDER: S-EPMC12262456 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature