Turingを超えるパターン形成：質量保存型反応拡散系の物理原理

Intracellular protein patterns govern essential cellular functions by dynamically redistributing proteins between membrane-bound and cytosolic states, conserving their total numbers. This review presents a theoretical framework for understanding such patterns based on mass-conserving reaction-diffusion systems. The emergence, selection, and evolution of patterns are analyzed in terms of mass redistribution and interface motion, resulting in mesoscale laws of coarsening and wavelength selection. A geometric phase-space perspective provides a conceptual tool to link local reactive equilibria with global pattern dynamics through conserved mass fluxes. The Min protein system of Escherichia coli provides a paradigmatic example, enabling direct comparison between theory and experiment. Successive model refinements capture both the robustness of pattern formation and the diversity of dynamic regimes observed in vivo and in vitro. The Min system thus illustrates how to extract predictive, multiscale theory from biochemical detail, providing a foundation for understanding pattern formation in more complex and synthetic systems.