Biophysical and structural studies reveal how low piconewton forces across actin enhance binding by the critical cell-cell adhesion protein α-catenin versus its force insensitive homolog vinculin.

Cryo-EM structures of actomyosin VI in multiple nucleotide states reveal a unique actin-myosin interface and a mechanism of force-sensitivity; furthermore, myosin VI remodels F-actin, suggesting a role for actin structural plasticity during force generation.

An actin-based Brownian Ratchet enables branched actin networks to generate pushing forces, while a capping protein-based Brownian Ratchet provides force feedback that enables these networks to adapt their architecture in response to changing loads.

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.

Deleting the first helix of the α-catenin actin-binding domain results in a slip bond interaction between the cadherin–catenin complex and F-actin, such that the binding interaction is stable at low force.

Computational modeling and single molecule imaging data support frequent disassembly and annealing of newly assembled actin, a process that can underlie structural changes of lamellipodial actin networks.

Live imaging of multiple cytoplasmic networks in frog egg extracts calls for new models for how egg cytoplasm is physically organized during cleavage divisions.

The dendrite branching receptor HPO-30 modulates actin dynamics by binding to both WAVE complex and actin filaments.

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

Structural, biochemical, and cell biology study revealed that Rsu1, through binding to PINCH1, inhibits the actin bundling ability of ILK/PINCH/Parvin to regulate the actin dynamics at focal adhesion.