Liquid-liquid phase separation in the tales of intrinsically disordered proteins

Jie-rong Huang^1*

¹Institute of Biochemistry and Molecular Biology, National Yang Ming Chiao Tung University, Taipei, Taiwan

* Presenter:Jie-rong Huang, email:jierongh@nycu.edu.tw

Proteins are the main workhorses in all lifeforms, responsible for a myriad of biological functions. A protein’s function depends on its three-dimensional shape. The various protein shapes merely depend on the linear arrangement of 20 “letters”, or “amino acids” in the language of proteins. How different linearly combined amino-acids codes for its structure was a “holy grail” in biology, but the recent machine-learning approach seems to get a good answer (AlphaFold). However, more than half of eukaryotic proteins have domains that do not fold into a well-defined structure, called intrinsically disordered proteins (IDPs) or proteins with intrinsically disordered regions (IDRs). How IDPs or IDRs function in the absence of a well-defined structure is just started to be understood. Many mechanisms have been reported for how IDPs/IDRs function, and a recent advance is that many of these proteins undergo liquid-liquid phase separation (LLPS) for spatiotemporal control of the location and timing of biological functions. Our group is interested in understanding the physicochemical properties of IDPs/IDRs and their relations to biological functions and diseases. In this talk, I will give an overview of the field of IDP/LLPS studies and some examples of our works.

Keywords: liquid-liquid phase separation, intrinsically disordered proteins, protein folding