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.

Single molecule imaging reveals how the molecular motor myosin 5 walks in a compass-like spinning motion along its actin track resulting in efficient, robust and unidirectional motion on the nanoscale.

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.

R788 is part of an allosteric communication pathway that connects the converter at the distal end of the myosin motor domain via the relay helix with switch-2 of the active site.

Components of a Spir:MyoV:Rab11 complex are recruited synergistically to coordinate actin tracks generation and myosin motor activity in vesicle transport processes.

Parvalbumin-positive inhibitory neurons in the cortex have insulating myelin sheathes, despite forming only short-range connections.

The small molecule EMD 57033 is one of a new class of pharmacological chaperones that stabilize, enhance the activity of, and correct stress-induced misfolding of myosin proteins.

Individual nonmuscle myosin 2 filaments in cells may differ their mechanical and kinetic properties depending on the myosin paralog composition giving the cells a mechanism for fine tuning the output of a given nonmuscle myosin filament.

PlexinD1 binding releases GIPC autoinhibition, leading to formation of high-order oligomers of the GIPC/myosin VI complex.

Atomic force microscopy based single-molecule force spectroscopy of smooth muscle myosin light chain kinase strongly indicates the existence of a mechanically triggerable activation pathway analogous to its well-established biochemical regulation pathway via calcium-loaded calmodulin.