Molecular interactions of poly(PR) dipeptides in liquid-liquid phase separation

摘要

Arginine-rich dipeptides repeat proteins (DPRs) encoded by a hexanucleotide expansion in C9ORF72 gene are known to be responsible for neurodegeneration in amyotrophic lateral sclerosis (ALS) [1, 2, 3]. These DRPs, along with RNA and other proteins, form liquid-liquid phase separation (LLPS) in cells, and impede functions of membrane-less organelles including nucleoli [4, 5], depending on their sequence [poly(PR) and poly(GR)]. However, the correlation between the primary peptide sequence and toxicity remains unclear.