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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.
Myosin-binding protein C (MyBP-C) resides and interacts with the myosin filaments in striated muscle and regulates contraction via an unclear mechanism. Here, the authors demonstrate that MyBP-C regulates the performance of myosin heads.
Fibroblasts actively search for and uptake microparticles from their environment and cells preferably uptake microdiamonds over latex beads. Myosin-X, EEA1 and microtubules are involved in this process.
Contractile ring formation, positioning, and closure is influenced by tissue mechanics, though how this information is transmitted is unclear. Here they show that Anillin is critical for a mechanosensitive pathway that drives cytokinesis and contractile ring closure.
The intricate molecular architecture and interactions of the human cardiac myosin filament offer insights into cardiac physiology, disease and drug therapy.
This study provides evidence that two RhoGEF isoforms displaying distinct localisation concurrently modulate Rho1 activity to promote robust furrow ingression while preserving cell size asymmetry during neural stem cell division.
Morphogenetic shape changes are regulated by mechanical properties of interacting tissues, but other factors remain less studied. By exploring how homeotic genes regulate morphogenesis, Villedieu et al. uncover how the interplay between genetic patterning and initial tissue geometry drives morphogenesis during development.
Engineered, light-inducible artificial myosin motors enable selective and direct manipulation of filopodial extensions and provide refined tools to control intracellular cargo transport in vivo.
Two independent studies now show that polymerization of branched actin at DNA double-strand breaks (DSBs) mediates chromatin dynamics associated with homology-directed repair and is required for a robust and error-free DSB repair process.
Two independent studies now show that polymerization of branched actin at DNA double-strand breaks (DSBs) mediates chromatin dynamics associated with homology-directed repair and is required for a robust and error-free DSB repair process.
Thomas D. Pollard discusses the early work of Thompson and Wolpert on cytoplasmic extract from amoebae, which laid the foundation for studies of actin-driven cell motility.
