Hsp90 and its co‐chaperone Sti1 control TDP‐43 misfolding and toxicity

Protein misfolding is a central feature of most neurodegenerative diseases. Molecular chaperones can modulate the toxicity associated with protein misfolding, but it remains elusive which molecular and co-chaperones interact specific misfolded proteins. TDP-43 inclusion formation are hallmark amyotrophic lateral sclerosis (ALS) other Using yeast mammalian neuronal cells we find that Hsp90 its co-chaperone Sti1 have capacity to alter formation, aggregation, cellular toxicity. Our data also demonstrate impaired function sensitizes specifically interacts strongly modulates in dose-dependent manner. study thus uncovers previously unrecognized tie between Hsp90, Sti1,