Partially overlapping functions of a limited subset of actin binding proteins allow the parasite Toxoplasma gondii to achieve actin regulation required for complex cellular processes.

The contractile ring actin binding proteins tropomyosin Cdc8 and a-actinin Ain1 synergize to effectively compete with the endocytic actin patch protein fimbrin Fim1 for associating with F-actin networks.

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.

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

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

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.

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.

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

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.

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.