Amandine Molliex

TL;DR: It is demonstrated that the disease-related RBP hnRNPA1 undergoes liquid-liquid phase separation (LLPS) into protein-rich droplets mediated by a low complexity sequence domain (LCD), and suggested that LCD-mediated LLPS contributes to the assembly of stress granules and their liquid properties.

TL;DR: Dysregulated polymerization caused by a potent mutant steric zipper motif in a PrLD can initiate degenerative disease and related proteins with PrLDs should be considered candidates for initiating and perhaps propagating proteinopathies of muscle, brain, motor neuron and bone.

TL;DR: It is demonstrated that phosphorylated or mutant aggregation prone recombinant tau undergoes LLPS, as does high molecular weight soluble phospho‐tau isolated from human Alzheimer brain, and it is suggested that LLPS represents a biophysical process with a role in multiple different neurodegenerative diseases.

TL;DR: It is found that arginine-containing DPRs, polyGly-Arg (GR) and polyPro- Arg (PR), interact with RNA-binding proteins and proteins with low complexity sequence domains (LCDs) that often mediate the assembly of membrane-less organelles.

TL;DR: A Drosophila model of VCP mutation-dependent degeneration is developed that is reminiscent of PINK1 and parkin mutants, including a pronounced mitochondrial defect, and it is shown that VCP recruitment to damaged mitochondria requires Parkin-mediated ubiquitination of mitochondrial targets.