Detailed studies of excitation contraction coupling allowed determination of quantitative relationships between resting potential, generation of action potentials, conduction of action potentials, and generation of Ca²⁺ transients in individual mouse skeletal muscle fibers.

Pericytes surrounding capillaries in the retina contain α-smooth muscle actin, demonstrating that pericytes have the necessary molecular machinery to change capillary diameter during neurovascular coupling.

The sequence of neural and physiological processes underlying action-stopping has been delineated.

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

Actin is incorporated into the thin-filament arrays of skeletal muscle sarcomeres in discrete steps, and Fhos, the Drosophila homolog of FHOD-family formins, is an essential player in the process.

Actin-related protein 5 antagonizes the interaction of Pbx/Meis with myogenic regulatory factors such as MyoD and MyoG, which is involved in the recruitment of the BRG1-based switch/sucrose nonfermentable chromatin remodeling complex required for myogenic gene activation.

Direct single molecule visualization of striated muscle relaxation using thin filament tightropes reveals the concerted release of myosins, with implications for models of muscle function.

Mutation E334Q in cytoskeletal γ-actin leads to impaired interaction of actin filaments with actin-binding proteins belonging to the myosin and ADF/cofilin families.

The epigenetic regulation of adult muscle stem cell fate by lnc-Rewind relies on the RNA-mediated recruitment of G9a methyltransferase on the Wnt7b genomic locus.

Integrative analysis of a Drosophila model of hypertrophic cardiomyopathy demonstrates that prolonged binding of the myosin cross-bridge to actin is a root cause of the disorder.