β- and γ-cytoplasmic actins have different translation rates in cells and exert different nucleotide coding sequence-dependent effects on cell migration.

Microtubules are nucleated by the centrosome of the primary cilium in the apical end-foot of neuroepithelial cells and inter-dependent microtubule and actin dynamics are required here to orchestrate delamination of newborn neurons.

Filopodia formation requires recruitment and activation of myosin through generation of parallel, bundled actin filaments by VASP polymerase, revealing coupling between motor activation and organization of a local actin network.

The movement of F-actin filaments, which is regulated by actin-myosin interactions together with a female gamete-specific Rho-GTPase, enables migration of the Arabidopsis sperm cell nucleus towards the female nucleus; which might account for the loss of centrosomes in flowering plants.

By restricting actin polymerization to the perimeter of the immune synapse and promoting depolymerization, calcium influx drives centripetal actin flow, which confines CRAC channels and the endoplasmic reticulum to the synapse center.

Real-time monitoring of oxytocin-loaded vesicles and synaptic actin dynamics in zebrafish reveal that Slit3-Robo2-Cdc42 signalling maintains steady-state levels of mature oxytocin neuropeptide readily primed to be secreted upon physiological demand.

Cells are able to control the actin network length and steering by adjusting geometric, structural, or biochemical parameters such as ADF/Cofilin and actin concentrations, and network width.

A key cellular process is controlled by altering a balance, rather than through an off/on mechanism.

The kinetics of actin polymerization are strongly influenced by the binding of proteins to the lateral filament surface.

Monomeric actin forms a crucial component of the eIF2α holophosphatase linking the integrated stress response to actin polymeric status.