Title:  Phase separation of RNA-binding proteins in neurodegenerative diseases

Cong Liu Ph.D

Email: liulab@sioc.ac.cn

 Abstract

Pathological amyloid fibrils are characteristic of highly thermostable cross-β structure. However, the stable cross-β architecture cannot explain the reversible amyloid fibrils formed by RNA-binding proteins such as hnRNPA1 and FUS that is involved in the dynamic assembly of stress granules. I will introduce our recent work on identification and structural characterization of highly reversible amyloid fibrils formed by hnRNPA1 and FUS by using our newly developed method – microED. Together with biochemical and cellular experiments, we demonstrated the essential role of reversible fibrils in phase separation and stress granule formation, dysregulation of which may lead to pathology in a variety of neurodegenerative diseases such as ALS and FTD.

 
Biography

 Dr. Cong Liu is currently a principal investigator at the interdisciplinary research center on biology and chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences. He obtained his Ph.D. degree from Peking University in 2008 and followed by postdoctoral training at UCLA&HHMI. He joined IRCBC in late 2013. His research interests include (1) Structural basis of pathological amyloid proteins aggregation including α-syn, Tau, FUS and hnRNPA1 which are key players in different neurodegenerative diseases (AD,PD and ALS); (2) Identification and characterization of liquid-liquid phase separation of different proteins involved in important biological process and pathology; (3) Method development for structural studies of amyloids aggregation and phase separation in vitro and in vivo (e.g. electron diffraction, in-cell NMR, IMMS); (4) Design of amyloid biomaterials with applicable functions. In the past five years, Dr. Liu has published over 20 papers related to protein phase separation including Cell, Nature Structural & Molecular Biology, Cell Research, Science Advances, Nature Communications and PNAS