Cellular viability requires tight regulation of actin cytoskeletal dynamics. Distinct families of
nucleation-promoting factors enable the rapid assembly of filament nuclei that elongate and …

Formins promote processive elongation of actin filaments for cytokinetic contractile rings and
other cellular structures. In vivo, these structures are exposed to tension, but the effect of …

When tagged with a fluorescent protein, actin is not fully functional 1 , so the LifeAct peptide
fused to a fluorescent protein is widely used to localize actin filaments in live cells 2 . …

Latrunculin A (LatA), a toxin from the red sea sponge Latrunculia magnifica, is the most widely
used reagent to depolymerize actin filaments in experiments on live cells. LatA binds actin …

Profilin binds not only to actin monomers but also to the barbed end of the actin filament,
where it inhibits association of subunits. To address open questions about the interactions of …

10.7554/eLife.48117.001 The microtubule binding protein EB1 specifically targets the growing
ends of microtubules in cells, where EB1 facilitates the interactions of cellular proteins …

Formins stimulate actin polymerization by promoting both filament nucleation and elongation.
Because nucleation and elongation draw upon a common pool of actin monomers, the rate …

Formin-mediated elongation of actin filaments proceeds via association of Formin Homology
2 (FH2) domain dimers with the barbed end of the filament, allowing subunit addition while …

Aip1 (actin interacting protein 1) is ubiquitous in eukaryotic organisms, where it cooperates
with cofilin to disassemble actin filaments, but neither its mechanism of action nor its …

Although our understanding of globular protein folding continues to advance, the irregular
tertiary structures and high cooperativity of globular proteins complicates energetic dissection. …