ArticleProceedings of the National Academy of Sciences of the United States of America2004
A one-headed class V myosin molecule develops multiple large (approximately 32-nm) steps successively.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed.
- Coupling of lever arm swing and biased Brownian motion in actomyosin.PLoS computational biology · 2014Article
- The loop2 insertion of type IX myosin acts as an electrostatic actin tether that permits processive movement.PloS one · 2014Article
- Article
- Myosin V passing over Arp2/3 junctions: branching ratio calculated from the elastic lever arm model.Biophysical journal · 2008Article
- Human myosin Vc is a low duty ratio nonprocessive motor.The Journal of biological chemistry · 2008Article
- Cargo-binding makes a wild-type single-headed myosin-VI move processively.Biophysical journal · 2006Article
- Lever arms and necks: a common mechanistic theme across the myosin superfamily.Journal of muscle research and cell motility · 2004Review
- The path to visualization of walking myosin V by high-speed atomic force microscopy.Biophysical reviewsArticle
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Authors and funding
9 authors.
Funding
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Abstract
Class V myosin (myosin-V) was first found as a processive motor that moves along an actin filament with large ( approximately 36-nm) successive steps and plays an important role in cargo transport in cells. Subsequently, several other myosins have also been found to move processively. Because myosin-V has two heads with ATP- and actin-binding sites, the mechanism of successive movement has been generally explained based on the two-headed structure. However, the fundamental problem of whether the two-headed structure is essential for the successive movement has not been solved. Here, we measure motility of engineered myosin-V having only one head by optical trapping nanometry. The results show that a single one-headed myosin-V undergoes multiple successive large (approximately 32-nm) steps, suggesting that a novel mechanism is operating for successive myosin movement.
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Registered trials
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