Abstract: Biomolecular condensates play a crucial role in organizing cellular architecture and regulating essential functions. Among these, ribonucleoprotein (RNP) granules represent a distinct class of condensates that assemble from RNA-binding proteins and RNA. In this talk, I will explore how the concept of biomolecular condensates has transformed our understanding of RNP granules and their links to disease, aging, and cellular stress responses.

I will introduce in vitro reconstitution systems based on phase separation, which now enable us to reconstruct RNP granules in a test tube. Leveraging these systems, along with advanced imaging techniques and biophysical approaches, we have uncovered key molecular principles governing RNP granule assembly. These include the driving forces and amino acid determinants of condensation, the conformational changes underlying assembly, and the molecular mechanisms that regulate condensate formation and function.

Furthermore, I will discuss how the condensate framework has provided new insights into the functional roles of RNP granules. Specifically, I will highlight how cells exploit condensate formation to sense environmental changes and regulate fundamental processes such as protein synthesis. By dissecting these mechanisms, we gain a deeper understanding of how biomolecular condensates contribute to cellular homeostasis and adaptation.