Exploring Structural Determinants and Functional Aspects of Micron-scale Protein Assemblies in Living Cells

Proteins are increasingly often seen as forming micron‐scale assemblies in their folded state. Such assemblies include, for example, CTP synthase, Glutamine synthase or Acetyl CoA carboxylase, all of which can form filaments under particular environmental or cellular conditions. Despite the rising prevalence of these micron‐scale structures, their structural basis and functional roles remain poorly understood at a cellular level. In particular, are there general structural principles underlying the formation of these assemblies? Is their accidental formation deleterious to cells? Do they naturally co‐localize with the quality‐control machinery of the cell? Does altering their formation impact cell fitness? To address these questions, we endogenously mutate several yeast proteins to either promote or inhibit their micron‐scale self‐assembly. We will present the results of these experiments, which provide answers to the questions posed above. Support or Funding Information European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme (grant agreement No. 819318)