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Myosins are a large family of cytoskeletal motor proteins that bind actin and use the energy of ATP hydrolysis to perform diverse functions such as cell motility and contractility, cytokinesis, intracellular trafficking and muscle contraction.
Thick filaments in skeletal muscle and heart are composed of myosin. The authors show that the length of thick filaments is defined by titin, and that alterations in titin length affect force generation and lead to dilated cardiomyopathy in mice.
The fission yeast cytokinetic ring assembles by Search-Capture-Pull-Release from precursor nodes that include formin Cdc12 and myosin Myo2. The authors reconstitute Search-Capture-Pull in vitro and find that Myo2 pulling on Cdc12-associated actin filaments mechano-inhibits Cdc12-mediated assembly, which enables proper ring assembly in vivo.
Spectacular images of the process of myosin II filament formation and organization in migrating cells are unveiled by super-resolution imaging. A combination of short- and long-range interactions with actin filaments is seen to play a critical role in filament partitioning and alignment into contractile actin arcs and stress fibres.
A powerful combination of cell labelling, genetic tools and rapid imaging techniques in vivo has now led to a high-resolution description of lumen formation during angiogenesis in zebrafish. The study reveals a haemodynamic-force-driven and myosin-II-dependent cellular mechanism (termed inverse membrane blebbing) as the basis for lumen expansion in unicellular and multicellular angiogenic sprouts.