Controlled Protein-Membrane Interactions Regulate Self-Organization of Min Protein Patterns

Self-organizing protein patterns play an essential role in life, governing important cellular processes, such as polarization and division. While the field of protein self-organization has reached a point where basic pattern-forming mechanisms can be reconstituted in vitro using purified proteins, understanding how cells can dynamically switch and modulate these patterns, especially when transiently needed, remains an interesting frontier. Here, we demonstrate the efficient regulation of self-organizing protein patterns through modulation of simple biophysical membrane parameters. Our investigation focusses on the impact of membrane affinity changes on Min protein patterns at lipid membranes composed of E. coli lipids or minimal lipid composition and we present three major results. First, we observed the emergence of a diverse array of pattern phenotypes, ranging from waves to snowflake-like structures. Second, we establish the dependency of these patterns on the density of protein-membrane linkers. Finally, we demonstrate the fine-tuning of snow-flake-like patterns by regulating membrane charge through lipid composition. Our results demonstrate the significant influence of membrane linkage as a straightforward biophysical parameter governing protein pattern formation. Our research points towards a simple yet intriguing mechanism by which cells can adeptly tune and switch protein patterns on the mesoscale.