The Honigmann group uses fluorescence imaging, in vitro reconstitution and organotypic tissue culture to study the supramolecular organization and function of cell-cell interfaces ^1,2. They discovered that the formation of tight junctions is driven by surface condensation of ZO scaffold proteins with adhesion receptors at cell-cell contacts^3,4. Structural analysis suggests that surface condensation leads to the assembly of an ordered mesoscale structure made of molecular layers of receptors, scaffolds, adapters and the cytoskeleton. Within the framework of the RTG, the Honigmann group will combine molecular reconstitutions and single molecule imaging with polymer physics to study how the surface condensation of scaffold proteins couples to conformational changes of proteins that are important for cortex regulation.

The Alberti group studies how cells adapt to environmental stresses by assembling biomolecular condensates. The group applies biophysical, biochemical, genetic, and cell biological methods to investigate the molecular mechanisms of assembly and the functions of stress inducible condensates. Among others, the Alberti group has shown that condensate assembly regulates protein synthesis^1-3, stress responses^1,2,4,5,6 and the DNA damage response^7,8. Most importantly, the Alberti group discovered together with the Hyman group that condensate-forming proteins can assemble into aberrant condensates that cause aging-associated diseases^7,6,9,10. In collaboration with the Schlierf group, the Alberti group recently established a model for the assembly of RNP granules and their function in regulating RNA availability and translation.