Mimicking two posttranslational modifications associated with oxidative stress affords phase separation of vimentin

The authors previously showed that vimentin filaments remodel into phase-separated condensates upon oxidative stress, a process dependent on the protein's single cysteine at position 328. Here, they test the hypothesis that oxidative modifications of C328, specifically sulfenylation or glutathionylation, trigger condensation. By generating vimentin variants that mimic these posttranslational modifications, they demonstrate that both modifications promote phase separation in cells. This links specific oxidative modifications to the biophysical behavior of an intermediate filament protein, potentially explaining how cells organize molecules during stress. The findings could inform future work on stress-responsive condensates and their role in diseases involving oxidative damage.