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.
An activator of branching nucleation by Arp2/3 complex directly synergizes with an activator of linear filament nucleation to initiate assembly of actin networks that drive endocytosis.
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.
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.
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.