16 research outputs found
A cycling state that can lead to glassy dynamics in intracellular transport
Power-law dwell times have been observed for molecular motors in living
cells, but the origins of these trapped states are not known. We introduce a
minimal model of motors moving on a two-dimensional network of filaments, and
simulations of its dynamics exhibit statistics comparable to those observed
experimentally. Analysis of the model trajectories, as well as experimental
particle tracking data, reveals a state in which motors cycle unproductively at
junctions of three or more filaments. We formulate a master equation for these
junction dynamics and show that the time required to escape from this
vortex-like state can account for the power-law dwell times. We identify trends
in the dynamics with the motor valency for further experimental validation. We
demonstrate that these trends exist in individual trajectories of myosin II on
an actin network. We discuss how cells could regulate intracellular transport
and, in turn, biological function, by controlling their cytoskeletal network
structures locally
Nucleation and shape dynamics of model nematic tactoids around adhesive colloids
Recent experiments have shown how nematically-ordered tactoid shaped actin
droplets can be reorganized and divided by the action of myosin molecular
motors. In this paper, we consider how similar morphological changes can
potentially be achieved under equilibrium conditions. Using simulations, both
atomistic and continuum, and a phenomenological model, we explore how the
nucleation dynamics, shape changes, and the final steady state of a nematic
tactoid droplet can be modified by interactions with model adhesive colloids
that mimic a myosin motor cluster. Our results provide a prescription for the
minimal conditions required to stabilize tactoid reorganization and division in
an equilibrium colloidal-nematic setting.Comment: 8 pages + appendice
Cycling State that Can Lead to Glassy Dynamics in Intracellular Transport
Power-law dwell times have been observed for molecular motors in living cells, but the origins of these trapped states are not known. We introduce a minimal model of motors moving on a two-dimensional network of filaments, and simulations of its dynamics exhibit statistics comparable to those observed experimentally. Analysis of the model trajectories, as well as experimental particle tracking data, reveals a state in which motors cycle unproductively at junctions of three or more filaments. We formulate a master equation for these junction dynamics and show that the time required to escape from this vortexlike state can account for the power-law dwell times. We identify trends in the dynamics with the motor valency for further experimental validation. We demonstrate that these trends exist in individual trajectories of myosin II on an actin network. We discuss how cells could regulate intracellular transport and, in turn, biological function by controlling their cytoskeletal network structures locally
Thermal Stress of Supported Lipid Bilayer Induces Formation and Collapse of Uniform Radius Tubules
Self-organization and shape change by active polarization in nematic droplets
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The Role of Bilayer Edges in Supported Lipid Bilayer Formation at Low Lipid Concentrations
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Self-organizing motors divide active liquid droplets
The cytoskeleton is a collection of protein assemblies that dynamically impose spatial structure in cells and coordinate processes such as cell division and mechanical regulation. Biopolymer filaments, cross-linking proteins, and enzymatically active motor proteins collectively self-organize into various precise cytoskeletal assemblies critical for specific biological functions. An outstanding question is how the precise spatial organization arises from the component macromolecules. We develop a system to investigate simple physical mechanisms of self-organization in biological assemblies. Using a minimal set of purified proteins, we create droplets of cross-linked biopolymer filaments. Through the addition of enzymatically active motor proteins, we construct composite assemblies, evocative of cellular structures such as spindles, where the inherent anisotropy drives motor self-organization, droplet deformation, and division into two droplets. These results suggest that simple physical principles underlie self-organization in complex biological assemblies and inform bioinspired materials design
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Tuning shape and internal structure of protein droplets via biopolymer filaments.
Macromolecules can phase separate to form liquid condensates, which are emerging as critical compartments in fields as diverse as intracellular organization and soft materials design. A myriad of macromolecules, including the protein FUS, form condensates which behave as isotropic liquids. Here, we investigate the influence of filament dopants on the material properties of protein liquids. We find that the short, biopolymer filaments of actin spontaneously partition into FUS droplets to form composite liquid droplets. As the concentration of the filament dopants increases, the coalescence time decreases, indicating that the dopants control viscosity relative to surface tension. The droplet shape is tunable and ranges from spherical to tactoid as the filament length or concentration is increased. We find that the tactoids are well described by a model of a quasi bipolar liquid crystal droplet, where nematic order from the anisotropic actin filaments competes with isotropic interfacial energy from the FUS, controlling droplet shape in a size-dependent manner. Our results demonstrate a versatile approach to construct tunable, anisotropic macromolecular liquids
Recommended from our members
Tuning shape and internal structure of protein droplets via biopolymer filaments.
Macromolecules can phase separate to form liquid condensates, which are emerging as critical compartments in fields as diverse as intracellular organization and soft materials design. A myriad of macromolecules, including the protein FUS, form condensates which behave as isotropic liquids. Here, we investigate the influence of filament dopants on the material properties of protein liquids. We find that the short, biopolymer filaments of actin spontaneously partition into FUS droplets to form composite liquid droplets. As the concentration of the filament dopants increases, the coalescence time decreases, indicating that the dopants control viscosity relative to surface tension. The droplet shape is tunable and ranges from spherical to tactoid as the filament length or concentration is increased. We find that the tactoids are well described by a model of a quasi bipolar liquid crystal droplet, where nematic order from the anisotropic actin filaments competes with isotropic interfacial energy from the FUS, controlling droplet shape in a size-dependent manner. Our results demonstrate a versatile approach to construct tunable, anisotropic macromolecular liquids