Profilin helps to maintain formin at the growing barbed end of an actin filament, while piconewton mechanical tension drastically enhances formin dissociation from the barbed end.

Formins slow elongation of actin filament by either sterically blocking the addition of actin subunits or flattening the helical twist of the filament end.

B-cell integrin co-stimulation promotes the formation of an actomyosin network that drives integrin-dependent immune synapse formation and B-cell activation.

siRNA knockdown experiments reveal in detail the signaling pathway that controls cytoskeletal function during cell-in-cell invasion.

Live-cell microscopy studies revealed that stress fibers can be generated de novo from the actin cortex without the involvement of stress fiber precursors.

Genetic and pharmacological tools are used to dissect the mechanisms by which the presynaptic actin cytoskeleton facilitates membrane internalization at synapses and, thereby, neurotransmission.

Profilin release from the filament end controls the speed of actin growth at physiological conditions.

On entry to meiosis, chromosomes scattered in the large oocyte nucleus of starfish are collected by an F-actin network, which contracts by an unexpected, myosin-independent mechanism based on local assembly and global disassembly of actin filaments.

Synergistic interactions with PI(4,5)P2 and activated Rho1, which are enriched at the apical membrane of tubular organs, facilitate tight apical targeting of the formin Diaphanous.

Fluorescently-tagged profilin-1 behaves similar to the tag-free protein in biochemical and cell-based assays.