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.

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.

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

The numerous reports in support of action-value representation in the striatum are based on statistical analyses that are subject to two critical confounds and, thus, this long-held belief of striatal action-value representation should be retested using different experiments and analyses.

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.

Compositional changes alter actin binding by phase separated T cell signaling clusters, enabling cluster movement by distinct actin networks.

At adhesion sites, talin-activated vinculin promotes interactions with the actin network that initiates bundles.

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.

An unbiased biochemical screen reveals a direct link between gene regulation and actin cytoskeleton remodeling.

Extracellular actin is an evolutionarily-conserved signal of tissue injury that is recognised in the fruit fly via similar machinery as reported in vertebrates.