Abstract

Intracellular protein patterns are described by (nearly) mass-conserving reaction-diffusion systems. While these patterns initially form out of a homogeneous steady state due to the well-understood Turing instability, no general theory exists for the dynamics of fully nonlinear patterns. We develop a unifying theory for nonlinear wavelength-selection dynamics in (nearly) mass-conserving two-component reaction-diffusion systems independent of the specific mathematical model chosen. Previous work has shown that these systems support an extremely broad band of stable wavelengths, but the mechanism by which a specific wavelength is selected has remained unclear. We show that an interrupted coarsening process selects the wavelength at the threshold to stability. Based on the physical intuition that coarsening is driven by competition for mass and interrupted by weak source terms that break strict mass conservation, we develop a singular perturbation theory for the stability of stationary patterns. The resulting closed-form analytical expressions enable us to quantitatively predict the coarsening dynamics and the final pattern wavelength. We find excellent agreement with numerical results throughout the diffusion- and reaction-limited regimes of the dynamics, including the crossover region. Further, we show how, in these limits, the two-component reaction-diffusion systems map to generalized Cahn-Hilliard and conserved Allen-Cahn dynamics, therefore providing a link to these two fundamental scalar field theories. The systematic understanding of the length-scale dynamics of fully nonlinear patterns in two-component systems provided here builds the basis to reveal the mechanisms underlying wavelength selection in multicomponent systems with potentially several conservation laws.

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