Proteasome condensates repeatedly "contact and release" at the nuclear periphery during dissolution.

Stress-induced proteasome condensates have been identified in both yeast and mammalian cells. The biochemical properties and dynamics of proteasome condensates mainly depend on the specific stress conditions. In the budding yeast , cytoplasmic proteasome condensates assemble from the nuclear proteasomes under glucose starvation conditions. Proteasome condensates rapidly dissipate, and proteasomes reimport to the nucleus within minutes upon glucose recovery. We characterize the kinetics and dynamics of proteasome condensates after glucose recovery. Proteasome condensates transiently associate nuclear membranes with a repetitive "contact and release" movement during dissolution. Our study provides new insight into the events leading to biomolecular condensate dissolution.