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1.
Phys Rev Lett ; 129(23): 238102, 2022 Dec 02.
Article in English | MEDLINE | ID: mdl-36563230

ABSTRACT

Cytoskeletal networks form complex intracellular structures. Here we investigate a minimal model for filament-motor mixtures in which motors act as depolymerases and thereby regulate filament length. Combining agent-based simulations and hydrodynamic equations, we show that resource-limited length regulation drives the formation of filament clusters despite the absence of mechanical interactions between filaments. Even though the orientation of individual remains fixed, collective filament orientation emerges in the clusters, aligned orthogonal to their interfaces.


Subject(s)
Cytoskeleton , Cytoskeleton/chemistry
2.
Biophys J ; 118(2): 313-324, 2020 01 21.
Article in English | MEDLINE | ID: mdl-31843261

ABSTRACT

Protein filament networks are structures crucial for force generation and cell shape. A central open question is how collective filament dynamics emerges from interactions between individual network constituents. To address this question, we study a minimal but generic model for a nematic network in which filament sliding is driven by the action of motor proteins. Our theoretical analysis shows how the interplay between viscous drag on filaments and motor-induced forces governs force propagation through such interconnected filament networks. We find that the ratio between these antagonistic forces establishes the range of filament interaction, which determines how the local filament velocity depends on the polarity of the surrounding network. This force-propagation mechanism implies that the polarity-independent sliding observed in Xenopus egg extracts and in vitro experiments with purified components is a consequence of a large force-propagation length. We suggest how our predictions can be tested by tangible in vitro experiments whose feasibility is assessed with the help of simulations and an accompanying theoretical analysis.


Subject(s)
Models, Molecular , Molecular Motor Proteins/chemistry , Molecular Motor Proteins/metabolism , Animals , Protein Conformation , Xenopus
3.
Sci Rep ; 7(1): 15420, 2017 11 13.
Article in English | MEDLINE | ID: mdl-29133925

ABSTRACT

The optical interaction of light and matter is modeled as an oscillating dipole in a plane wave electromagnetic field. We analyze absorption, scattering and extinction for this system by the energy flow, visualized as streamlines of the Poynting vector. Depending on the dissipative damping of the oscillator, a part of the streamlines ends up in the dipole. Based on a graphical investigation of the streamlines, this represents the absorption cross section, and forms a far-field absorption aperture. In the near-field of the oscillator, a modification of the aperture is observed. As in the case for a linear dipole, we model the energy flow and derive the effective absorption apertures for an oscillator with a circular dipole characteristics - such as an atom in free space.

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