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

Cryo-EM structures of actomyosin VI in multiple nucleotide states reveal a unique actin-myosin interface and a mechanism of force-sensitivity; furthermore, myosin VI remodels F-actin, suggesting a role for actin structural plasticity during force generation.

Computational simulations of actin network growth at the cell leading edge, combined with careful high-speed video microscopy measurements of leading edge shape fluctuations, suggest that Arp2/3 branching of the actin network occurs at an optimal angle to minimize fluctuations.

Biophysical and structural studies reveal how low piconewton forces across actin enhance binding by the critical cell-cell adhesion protein α-catenin versus its force insensitive homolog vinculin.

The functional differences between actin isoforms have been explored through structural studies.

Combination of actin and curly on lipid membranes constitutes a new, minimalistic system to generate high curvature actin rings that can contract upon the action of myosin II filaments.

Neurotrophin deprivation leads to rapid caspase-independent disassembly of the actin-spectrin-based membrane skeleton and spectrin-dependent retrograde signaling in axon degeneration.

Fat-body-specific loss of actin isoform Act5C disrupts fat body cell growth and fat storage, lipoprotein secretion, and insulin signaling, revealing a non-canonical role for the cortical actin cytoskeleton in nutrient signaling and inter-organelle trafficking.

Structural research, supplemented by biochemical experiments and enzymatic assays, unravels the sequence-dependent molecular mechanism by which SETD3 recognizes β-actin and methylates His73 of β-actin.

A molecular mechanism for force-dependent binding of the cell adhesion proteins αE-catenin and vinculin to actin is derived from the structure of the αE-catenin actin-binding domain bound to F-actin.