The tail domain of Myosin III binds to and cross-links actin bundling protein Espin1 and thus modulates higher order actin bundle structures in cellular processes such as stereocilia and microvilli.

Epsin has a key role in the coupling of actin to endocytic clathrin coated pits that is required for their maturation and helps capture SNAREs at endocytic clathrin coated pits.

Kinesin-like calmodulin-binding protein integrates microtubules and F-actin to assemble the cytoskeletal configuration needed for trichome formation.

An efficient response to DNA damage requires the assembly of actin filaments in the nucleus.

T cell receptor signaling is regulated by newly polymerized F-actin foci at the immunological synapse.

A cluster of cofilin along an otherwise bare actin filament induces distinctively asymmetric cooperative conformational changes to the filament on either side of the cluster.

A combination of imaging experiments and computer simulations on a model lipid membrane integrate the 'picket fence' and 'raft' models, and suggest that the interplay between actin binding, lipid phase separation and curvature compartmentalize the membrane.

A combination of single-molecule imaging and an in vitro model of the cell cortex has allowed the interactions between actin filaments and filaments made of myosin II to be studied in detail.

Cytological and biochemical analyses reveal Arabidopsis formin 2 is involved in regulating PD permeability by anchoring actin filaments to PD and stabilizing them through actin filament barbed end capping activity.

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.