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.

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.

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.

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.

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.