ArticleProceedings of the National Academy of Sciences of the United States of America2014
Motor coupling through lipid membranes enhances transport velocities for ensembles of myosin Va.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- The unconventional regulation of non-muscle myosins.Biophysical reviews · 2026Article
- Kinesin-1 autoinhibition tunes cargo transport by motor ensembles.Biophysical journal · 2025Article
- Motor clustering enhances kinesin-driven vesicle transport.Biophysical journal · 2025Article
- Stick-slip motion and universal statistics of cargo transport within living cells.bioRxiv : the preprint server for biology · 2025Article
- Kinesin-1-transported liposomes prefer to go straight in 3D microtubule intersections by a mechanism shared by other molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Phosphatidic acid-dependent recruitment of microtubule motors to spherical supported lipid bilayers for in vitro motility assays.Cell reports · 2024Article
- Vesicles driven by dynein and kinesin exhibit directional reversals without regulators.Nature communications · 2023Article
- Cholesterol in the cargo membrane amplifies tau inhibition of kinesin-1-based transport.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cargo surface fluidity can reduce inter-motor mechanical interference, promote load-sharing and enhance processivity in teams of molecular motors.PLoS computational biology · 2022Article
- Modeling myosin Va liposome transport through actin filament networks reveals a percolation threshold that modulates transport properties.Molecular biology of the cell · 2022Article
- Diffusion of kinesin motors on cargo can enhance binding and run lengths during intracellular transport.Molecular biology of the cell · 2021Article
- Article
- Estimating numbers of intracellular molecules through analysing fluctuations in photobleaching.Scientific reports · 2019Article
- Article
- Membrane mediated motor kinetics in microtubule gliding assays.Scientific reports · 2019Article
- Article
- Myosin Va transport of liposomes in three-dimensional actin networks is modulated by actin filament density, position, and polarity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Intracellular cargo transport by single-headed kinesin motors.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Cargo diffusion shortens single-kinesin runs at low viscous drag.Scientific reports · 2019Article
- Dissecting myosin-5B mechanosensitivity and calcium regulation at the single molecule level.Nature communications · 2018Article
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3 authors.
Funding
Abstract
Myosin Va is an actin-based molecular motor responsible for transport and positioning of a wide array of intracellular cargoes. Although myosin Va motors have been well characterized at the single-molecule level, physiological transport is carried out by ensembles of motors. Studies that explore the behavior of ensembles of molecular motors have used nonphysiological cargoes such as DNA linkers or glass beads, which do not reproduce one key aspect of vesicular systems--the fluid intermotor coupling of biological lipid membranes. Using a system of defined synthetic lipid vesicles (100- to 650-nm diameter) composed of either 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) (fluid at room temperature) or 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) (gel at room temperature) with a range of surface densities of myosin Va motors (32-125 motors per μm(2)), we demonstrate that the velocity of vesicle transport by ensembles of myosin Va is sensitive to properties of the cargo. Gel-state DPPC vesicles bound with multiple motors travel at velocities equal to or less than vesicles with a single myosin Va (∼450 nm/s), whereas surprisingly, ensembles of myosin Va are able to transport fluid-state DOPC vesicles at velocities significantly faster (>700 nm/s) than a single motor. To explain these data, we developed a Monte Carlo simulation that suggests that these reductions in velocity can be attributed to two distinct mechanisms of intermotor interference (i.e., load-dependent modulation of stepping kinetics and binding-site exclusion), whereas faster transport velocities are consistent with a model wherein the normal stepping behavior of the myosin is supplemented by the preferential detachment of the trailing motor from the actin track.
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