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- W2023772919 startingPage "5820" @default.
- W2023772919 abstract "The force generated between actin and myosin acts predominantly along the direction of the actin filament, resulting in relative sliding of the thick and thin filaments in muscle or transport of myosin cargos along actin tracks. Previous studies have also detected lateral forces or torques that are generated between actin and myosin, but the origin and biological role of these sideways forces is not known. Here we adapt an actin gliding filament assay to measure the rotation of an actin filament about its axis (“twirling”) as it is translocated by myosin. We quantify the rotation by determining the orientation of sparsely incorporated rhodamine-labeled actin monomers, using polarized total internal reflection microscopy. To determine the handedness of the filament rotation, linear incident polarizations in between the standard s- and p-polarizations were generated, decreasing the ambiguity of our probe orientation measurement fourfold. We found that whole myosin II and myosin V both twirl actin with a relatively long (∼1 μm), left-handed pitch that is insensitive to myosin concentration, filament length, and filament velocity." @default.
- W2023772919 created "2016-06-24" @default.
- W2023772919 creator A5013832205 @default.
- W2023772919 creator A5063612088 @default.
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- W2023772919 date "2008-12-01" @default.
- W2023772919 modified "2023-09-26" @default.
- W2023772919 title "Twirling of Actin by Myosins II and V Observed via Polarized TIRF in a Modified Gliding Assay" @default.
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- W2023772919 doi "https://doi.org/10.1529/biophysj.108.140319" @default.
- W2023772919 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2599829" @default.
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