Jinge Gu

TL;DR: The authors identify reversible amyloid cores from the LC of hnRNPA1, based on which they elucidate the structural basis of reversible fibrillation and its interplay with hn RNPA1 droplet formation.

TL;DR: A novel and crucial role is suggested for PARylation in regulating the dynamics of RNP granules, and that dysregulation inPARylation and PAR levels may contribute to ALS disease pathogenesis by promoting protein aggregation.

TL;DR: These motifs reversible amyloid cores are named, or RAC1 and RAC2, and their atomic structures in fibrillar forms are determined, which illuminate the mechanism of reversible fibril formation and dynamic assembly of RNA granules.

TL;DR: This work finds that human small heat-shock protein 27 (Hsp27), a canonical chaperone that localizes to stress granules (SGs), prevents FUS from undergoing liquid−liquid phase separation (LLPS) via weak interactions with the FUS low complexity (LC) domain and suggests an essential role for Hsp27 in stabilizing the dynamic phase of stress granule.

TL;DR: An unexpected role is reported in the formation of dynamic, reversible, liquid droplet-like nuclear bodies (NBs) in response to stress, which suggests a stress-mitigating role and mechanism of TDP-43 NBs, whose dysfunction may be involved in ALS pathogenesis.