Living in a bubble

In our cells, proteins assemble into amazingly dynamic macromolecular machines whose function and regulation underlie life’s essential processes. A perfect example is gene expression, in which cells depend on versatile biomolecular machines to harness the information in DNA.

Understanding the inner workings of these intricate assemblies is among the great challenges in the biomedical sciences. Knowledge was, until recently, severely limited by their sizes and complexity.

Therefore, our field has been greatly excited by the incredible advances in cryo-electron microscopy and its “resolution revolution,” which we will feature in our symposia at the American Society for Biochemistry and Molecular Biology annual meeting, Discover BMB, in Seattle in March.

A contrast to the highly structured protein complexes lies in the often underappreciated structurally disordered protein regions, which also will be in in the limelight during our symposia. Recent studies have shown that, far from being useless, these disordered regions can cause liquid–liquid phase separation — an omnipresent phenomenon in eukaryotic cells underpinning the formation of membraneless organelles.

Localization of protein machines within membraneless organelles allows them to work more efficiently or achieve necessary regulatory interactions. Conversely, condensate disruption compromises the function of the protein machines within, leading to human diseases.

Keywords: Protein complexes, gene expression, genome maintenance, intrinsically disordered regions, lipid–lipid phase separation, computational biology, cancer, neurodegeneration.

Who should attend: Anyone who works with proteins with ordered or disordered regions. (Well, isn’t that everybody?)

Theme song: “With a Little Help from My Friends” by the Beatles. (The protein machines work so efficiently with the help of the condensates formed by disordered regions of the proteins.)

This session is powered by structured proteins (yang) and droplets (yin).