ArticleScientific reports2014
Coupling of two non-processive myosin 5c dimers enables processive stepping along actin filaments.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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
9 citing papers in PubMed, 18 citations in OpenAlex.
- Motor properties of Myosin 5c are modulated by tropomyosin isoforms and inhibited by pentabromopseudilin.Frontiers in physiology · 2024Article
- Methylome-wide association study of central adiposity implicates genes involved in immune and endocrine systems.Epigenomics · 2020Article
- Dissecting myosin-5B mechanosensitivity and calcium regulation at the single molecule level.Nature communications · 2018Article
- Kinetic signatures of myosin-5B, the motor involved in microvillus inclusion disease.The Journal of biological chemistry · 2017Article
- Small teams of myosin Vc motors coordinate their stepping for efficient cargo transport on actin bundles.The Journal of biological chemistry · 2017Article
- Embedding dual function into molecular motors through collective motion.Scientific reports · 2017Article
- Myosin Vc Is Specialized for Transport on a Secretory Superhighway.Current biology : CB · 2016Article
- Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.Traffic (Copenhagen, Denmark) · 2016Review
- Identification of the Isoform-specific Interactions between the Tail and the Head of Class V Myosin.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Myosin 5c (Myo5c) is a low duty ratio, non-processive motor unable to move continuously along actin filaments though it is believed to participate in secretory vesicle trafficking in vertebrate cells. Here, we measured the ATPase kinetics of Myo5c dimers and tested the possibility that the coupling of two Myo5c molecules enables processive movement. Steady-state ATPase activity and ADP dissociation kinetics demonstrated that a dimer of Myo5c-HMM (double-headed heavy meromyosin 5c) has a 6-fold lower Km for actin filaments than Myo5c-S1 (single-headed myosin 5c subfragment-1), indicating that the two heads of Myo5c-HMM increase F-actin-binding affinity. Nanometer-precision tracking analyses showed that two Myo5c-HMM dimers linked with each other via a DNA scaffold and moved processively along actin filaments. Moreover, the distance between the Myo5c molecules on the DNA scaffold is an important factor for the processive movement. Individual Myo5c molecules in two-dimer complexes move stochastically in 30-36 nm steps. These results demonstrate that two dimers of Myo5c molecules on a DNA scaffold increased the probability of rebinding to F-actin and enabled processive steps along actin filaments, which could be used for collective cargo transport in cells.
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Registered trials
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