Liquidizing FUS via prion‐like domain phosphorylation

Abstract

© 2017 EMBO. FUS is an RNA-binding protein (RBP) with a prion-like domain (PrLD) that condenses into functional liquids, which can aberrantly phase transition into solid aggregates comprised of pathological fibrils connected to neurodegenerative disease. How cells prevent aberrant phase transitions of FUS and other disease-linked RBPs with PrLDs is poorly understood. In this issue of The EMBO Journal, Monahan et al () establish that phosphorylation of specific serine and threonine residues in the FUS PrLD inhibits aberrant phase separation and toxicity.