Multistability and dynamic transitions of intracellular Min protein patterns
In this work, we probe a fundamental question in cellular and developmental biology: how do self-organized (Turing) protein patterns evolve with cell growth and achieve robustness in a fluctuating environment? Whereas studies on the effect of noise and boundary growth on cellular metabolism have lead to great advances in the past decade, our understanding of dynamic spatial organization is lagging behind in this context despite its pervasive importance. Essentially, adding geometric perturbations and spatial heterogeneity to the already complex problems of spatio-temporal patterns easily drives them beyond the accessibility of present approaches. Here we use a combination of complementary experimental and theoretical approaches to dissect the mechanisms that drive the robustness and adaptation of division-regulator Min protein patterns.
The nanoengineering method combined with quantitative imaging reveals a novel multistability phenomenon with surprising properties including extreme robustness and dynamic transitions between distinctly different patterns. Analytical and computational work demonstrates how symmetry breaking should be treated without bias in realistic biological geometries, and explains the origin of the observed multistability through probing the effect of spatial perturbations in a large kinetic and geometric parameter space. Altogether, our findings demonstrate that the boundary-pattern relation during growth and pattern robustness against fluctuations can be hardwired in the chemical basis of pattern formation systems. Thus basic rules can be derived through systems approaches to explain these complex biological phenomena. This has far-reaching implications for dynamic pattern formation in cellular and developmental processes in general.