While acetylated, RNA-binding-deficient TDP-43 reversibly phase separates within nuclei
into complex droplets (anisosomes) comprised of TDP-43-containing liquid outer shells and
liquid centres of HSP70-family chaperones, cytoplasmic aggregates of TDP-43 are
hallmarks of multiple neurodegenerative diseases, including amyotrophic lateral sclerosis
(ALS). Here we show that transient oxidative stress, proteasome inhibition or inhibition of the
ATP-dependent chaperone activity of HSP70 provokes reversible cytoplasmic TDP-43 de …

While the RNA binding protein TDP-43 reversibly phase separates within nuclei into
complex droplets (anisosomes) with TDP-43-containing liquid outer shells and liquid centers
of HSP70 family chaperones, cytoplasmic aggregates of TDP-43 are hallmarks of multiple
neurodegenerative diseases, including ALS. Here we show that transient oxidative stress,
proteasome inhibition, or inhibition of HSP70's ATP-dependent chaperone activity provokes
reversible cytoplasmic TDP-43 de-mixing and transition from liquid to gel/solid, independent …