Low-dimensional manifold of actin polymerization dynamics
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Publication:6204512
DOI10.1088/1367-2630/AA9641arXiv1708.04695OpenAlexW3100423991WikidataQ62126160 ScholiaQ62126160MaRDI QIDQ6204512FDOQ6204512
Authors: Christopher Jarzynski, Garegin A. Papoian 
Publication date: 28 March 2024
Published in: New Journal of Physics (Search for Journal in Brave)
Abstract: Actin filaments are critical components of the eukaryotic cytoskeleton, playing important roles in a number of cellular functions, such as cell migration, organelle transport, and mechanosensation. They are helical polymers with a well-defined polarity, composed of globular monomers that bind nucleotides in one of three hydrolysis states (ATP, ADP-Pi, or ADP). Mean-field models of the dynamics of actin polymerization have succeeded in, among other things, determining the nucleotide profile of an average filament and resolving the mechanisms of accessory proteins, however these models require numerical solution of a high-dimensional system of nonlinear ODE's. By truncating a set of recursion equations, the Brooks-Carlsson model reduces dimensionality to 11, but it remains nonlinear and does not admit an analytical solution, hence, significantly hindering understanding of its resulting dynamics. In this work, by taking advantage of the fast timescales of the hydrolysis states of the filament tips, we propose two model reduction schemes that achieve low dimensionality and linearity. We provide an exact solution of the resulting linear equations and use it to shed light on the dynamical behaviors of the full BC model, highlighting the relative ordering of the timescales of various collective processes, and explaining some unusual dependence of the steady-state behavior on initial conditions.
Full work available at URL: https://arxiv.org/abs/1708.04695
Statistical mechanics, structure of matter (82-XX) Quantum theory (81-XX) Relativity and gravitational theory (83-XX)
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