ArticleBiophysical journal2006
Cargo-binding makes a wild-type single-headed myosin-VI move processively.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 58 citations in OpenAlex.
- Autoinhibition and activation of myosin VI revealed by its cryo-EM structure.Nature communications · 2024Article
- Autoregulation and dual stepping mode of MYA2, an Arabidopsis myosin XI responsible for cytoplasmic streaming.Scientific reports · 2022Article
- Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.Traffic (Copenhagen, Denmark) · 2016Review
- The cortical acto-Myosin network: from diffusion barrier to functional gateway in the transport of neurosecretory vesicles to the plasma membrane.Frontiers in endocrinology · 2013Review
- Muscle contraction mechanism based on single molecule measurements.Journal of muscle research and cell motility · 2012Article
- Membrane-induced lever arm expansion allows myosin VI to walk with large and variable step sizes.The Journal of biological chemistry · 2012Article
- Myosin VI contributes to synaptic transmission and development at the Drosophila neuromuscular junction.BMC neuroscience · 2011Article
- Lever-arm mechanics of processive myosins.Biophysical journal · 2011Review
- Nucleotide-dependent shape changes in the reverse direction motor, myosin VI.Biophysical journal · 2010Article
- Article
- One-dimensional Brownian motion of charged nanoparticles along microtubules: a model system for weak binding interactions.Biophysical journal · 2010Article
- Single-molecule stepping and structural dynamics of myosin X.Nature structural & molecular biology · 2010Article
- Myosin VI: an innovative motor that challenged the swinging lever arm hypothesis.Nature reviews. Molecular cell biology · 2010Review
- Engineered myosin VI motors reveal minimal structural determinants of directionality and processivity.Journal of molecular biology · 2009Article
- Brownian search-and-catch mechanism for myosin-VI steps.Nature chemical biology · 2009Article
- Coiled-coil-mediated dimerization is not required for myosin VI to stabilize actin during spermatid individualization in Drosophila melanogaster.Molecular biology of the cell · 2009Article
- Single molecule measurements and molecular motors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2008Review
- Myosin V and Kinesin act as tethers to enhance each others' processivity.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Myosin VI walks "wiggly" on actin with large and variable tilting.Molecular cell · 2007Article
- Violation of the fluctuation-dissipation theorem in a protein system.Biophysical journal · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Class VI myosin is an intracellular vesicle and organelle transporter that moves along actin filaments in a direction opposite to most other known myosin classes. The myosin-VI was expected to form a dimer to move processively along actin filaments with a hand-over-hand mechanism like other myosin organelle transporters. Recently, however, wild-type myosin-VI was demonstrated to be monomer and single-headed, casting a doubt on its processivity. By using single molecule techniques, we show that green-fluorescent-protein-tagged single-headed, wild-type myosin-VI does not move processively. However, when coupled to 200-nm polystyrene beads (comparable to intracellular vesicles in size) at a ratio of one head per bead, single-headed myosin-VI moves processively with large (40-nm) steps. The characteristics of this monomer-driven movement were different to that of artificial dimer-driven movement: Compared to the artificial dimer, the monomer-bead complex had a reduced stall force (1 pN compared to 2 pN), an average run length 2.5-fold shorter (91 nm compared to 220 nm) and load-dependent step size. Furthermore, we found that a monomer-bead complex moved more processively in a high viscous solution (40-fold higher than water) similar to cellular environment. Because the diffusion constant of the bead is 60-fold lower than myosin-VI heads alone in water, we propose a model in which the bead acts as a diffusional anchor for the myosin-VI, enhancing its rebinding following detachment and supporting processive movement of the bead-monomer complexes. Although a single-headed myosin-VI was able to move processively with a large cargo, the travel distance was rather short. Multiple molecules may be involved in the cargo transport for a long travel distance in cells.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.