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.

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.

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.

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

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

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.

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.

Acquisition of behavioral sequences in normally aged mice involves short and unusually fast patterns of action, some of which are reproduced by striatal circuitry manipulations in young mice and can be transitorily restored through action-related feedback.