Stall force of polymerizing microtubules and filament bundles

Krawczyk, J.; Kierfeld, Jan

doi:10.1209/0295-5075/93/28006

Cited by 35 publications

(77 citation statements)

References 29 publications

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“…Some arguments, based on detailed balance criterion, have also been given in Refs. [26] and [29] to show similar result of f (N ) s ∝ N for their respective models on cytoskeletal filaments. However, we demonstrate that a simple calculation based on elementary statistical mechanics, for essentially kinetic processes, leads to the same conclusion.…”

Section: Collective Stall Force For Multiple Cytoskeletal Filamensupporting

confidence: 52%

“…On the theoretical and computational front, there are a number of very detailed models for understanding the force-velocity dynamics of a single biofilament [50][51][52][53], as well as a few that try to model the dynamics of multiple biofilaments [26,[28][29][30][31][54][55][56]. Some of these theoretical studies have demonstrated that the stall force of multiple, non-interacting filaments without ATP/GTP dynamics, scales linearly with the number of filaments [26,[28][29][30]54].…”

Section: Introductionmentioning

confidence: 99%

“…Some of these theoretical studies have demonstrated that the stall force of multiple, non-interacting filaments without ATP/GTP dynamics, scales linearly with the number of filaments [26,[28][29][30]54]. In contrast, a few other recent papers quite clearly report that inclusion of ATP/GTP hydrolysis can lead to either enhanced or reduced cooperativity in the maximum force generated by multiple growing filaments; the stall forces need not always scale with the number of filaments [31,[56][57][58].…”

Section: Introductionmentioning

confidence: 99%

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Sufficient conditions for the additivity of stall forces generated by multiple filaments or motors

Bameta

Das

et al. 2017

Phys. Rev. E

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Molecular motors and cytoskeletal filaments work collectively most of the time under opposing forces. This opposing force may be due to cargo carried by motors or resistance coming from the cell membrane pressing against the cytoskeletal filaments. Some recent studies have shown that the collective maximum force (stall force) generated by multiple cytoskeletal filaments or molecular motors may not always be just a simple sum of the stall forces of the individual filaments or motors. To understand this excess or deficit in the collective force, we study a broad class of models of both cytoskeletal filaments and molecular motors. We argue that the stall force generated by a group of filaments or motors is additive, that is, the stall force of N number of filaments (motors) is N times the stall force of one filament (motor), when the system is in equilibrium at stall. Conversely, we show that this additive property typically does not hold true when the system is not at equilibrium at stall. We thus present a novel and unified understanding of the existing models exhibiting such nonaddivity, and generalise our arguments by developing new models that demonstrate this phenomena. We also propose a quantity similar to thermodynamic efficiency to easily predict this deviation from stall-force additivity for filament and motor collectives.

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Section: Collective Stall Force For Multiple Cytoskeletal Filamensupporting

confidence: 52%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Sufficient conditions for the additivity of stall forces generated by multiple filaments or motors

Bameta

Das

et al. 2017

Phys. Rev. E

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“…The ability of actin filaments to sustain in supercritical conditions a compressive force has predominantly been justified with the aid of the rigid living filament model, effectively a one dimensional model, both for the single filament case and for bundles of parallel filaments [4,[6][7][8][9][10][11][12][13]. The 1D filaments which are fluctuating in length as a result of (de)polymerizing steps are hitting a fluctuating obstacle usually subject to load by producing instantaneous kicks which result into a time averaged force biasing the obstacle brownian motion.…”

Section: Resultsmentioning

confidence: 99%

A semi-flexible model prediction for the polymerization force exerted by a living F-actin filament on a fixed wall

Pierleoni

Ciccotti

Ryckaert

2015

The Journal of Chemical Physics

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We consider a single living semi-flexible filament with persistence length p in chemical equilibrium with a solution of free monomers at fixed monomer chemical potential µ1 and fixed temperature T . While one end of the filament is chemically active with single monomer (de)polymerization steps, the other end is grafted normally to a rigid wall to mimick a rigid network from which the filament under consideration emerges. A second rigid wall, parallel to the grafting wall, is fixed at distance L << p from the filament seed. In supercritical conditions where monomer density ρ1 is higher than the critical density ρ1c, the filament tends to polymerize and impinges onto the second surface which, in suitable conditions (non-escaping filament regime) stops the filament growth. We first establish the grand-potential Ω(µ1, T, L) of this system treated as an ideal reactive mixture and derive some general properties, in particular the filament size distribution and the force exerted by the living filament on the obstacle wall. We apply this formalism to the semi-flexible, living, over a compression range much narrower than the size d of a monomer. Employing this universal form for living filaments, we find that the average force exerted by a living filament on a wall at distance L is in practice L independent and very close to the value of the stalling force F H s = (kBT /d) ln(ρ1) predicted by Hill, this expression being strictly valid in the rigid filament limit. The average filament force results from the product of the cumulative size fraction

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“…[6][7][8][9][10][11][12][13][14] To do so, extant theories (and many simulations as well) have appealed to approximations that are not generally justified by the underlying chemical kinetics. For example, it is commonly assumed that nonequilibrium considerations are important only for the discrete, driven part of the ratcheting process; all other degrees of freedom are imagined to follow adiabatically.…”

mentioning

confidence: 99%

Nanoscale dynamics and aging of fibrous peptide-based gels

Dudukovic

Zukoski

2014

The Journal of Chemical Physics

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Solutions of the aromatic dipeptide derivative molecule fluorenylmethoxycarbonyl-diphenylalanine (Fmoc-FF) in dimethyl sulfoxide produce fibrous gels when mixed with water. We study the evolution of density fluctuations of this three-component system using X-ray photon correlation spectroscopy (XPCS) and compare these results to the macroscopic rheology of the gels and optical observations of the microstructure evolution. At the investigated scattering angles, the intensity autocorrelation functions do not follow behavior expected for simple diffusion of individual Fmoc-FF molecules localized within cages of nearest neighbors. Instead, the dynamics are associated with density fluctuations on length scales of ∼10–100 nm arising from disaggregation and reformation of fibers, leading to an increasingly uniform network. This process is correlated with the growth of the elastic modulus, which saturates at long times. Autocorrelation functions and relaxation times acquired from XPCS measurements are consistent with relaxation rates of structures at dynamic equilibrium. This study provides further support to the concept of exploring peptide-based gelators as valence-limited patchy particles capable of forming equilibrium gels.

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Stall force of polymerizing microtubules and filament bundles

Cited by 35 publications

References 29 publications

Sufficient conditions for the additivity of stall forces generated by multiple filaments or motors

Sufficient conditions for the additivity of stall forces generated by multiple filaments or motors

A semi-flexible model prediction for the polymerization force exerted by a living F-actin filament on a fixed wall

Nanoscale dynamics and aging of fibrous peptide-based gels

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