Effects of geometry and topography on Min-protein dynamics.

In the rod-shaped bacterium Escherichia coli, the center is selected by the Min-proteins as the site of cell division. To this end, the proteins periodically translocate between the two cell poles, where they suppress assembly of the cell division machinery. Ample evidence notably obtained from in vitro reconstitution experiments suggests that the oscillatory pattern results from self-organization of the proteins MinD and MinE in presence of a membrane.

C2-domain mediated nano-cluster formation increases calcium signaling efficiency.

Conventional protein kinase Cs (cPKCs) are key signaling proteins for transducing intracellular Ca signals into downstream phosphorylation events. However, the lifetime of individual membrane-bound activated cPKCs is an order of magnitude shorter than the average time needed for target-protein phosphorylation. Here, we employed intermolecular Förster resonance energy transfer (FRET) in living cells combined with computational analysis to study the spatial organization of cPKCs bound to the plasma membrane.

Membrane binding of MinE allows for a comprehensive description of Min-protein pattern formation.

The rod-shaped bacterium Escherichia coli selects the cell center as site of division with the help of the proteins MinC, MinD, and MinE. This protein system collectively oscillates between the two cell poles by alternately binding to the membrane in one of the two cell halves. This dynamic behavior, which emerges from the interaction of the ATPase MinD and its activator MinE on the cell membrane, has become a paradigm for protein self-organization.

Geometry sensing by self-organized protein patterns.

In the living cell, proteins are able to organize space much larger than their dimensions. In return, changes of intracellular space can influence biochemical reactions, allowing cells to sense their size and shape. Despite the possibility to reconstitute protein self-organization with only a few purified components, we still lack knowledge of how geometrical boundaries affect spatiotemporal protein patterns.