Dsk2 is a yeast protein that contains small domains interspersed with disordered segments, including regions with low complexity. In vitro (NMR, phase transition experiments), we found that the yeast protein Dsk2 contains small transient helices in its disordered regions and that these, along with its STI1 domain, contribute to Dsk2’s liquid-liquid phase separation more than its other domains. However, in vivo, determining the relative contributions of Dsk2’s domains and disordered regions was more complicated, as there were pleiotropic effects with deleting the STI1 domain or the three transient helices. Ultimately, we showed that the STI1 domain likely facilitates the degradation of proteins via the proteasome even without exogenous stress, and its deletion increased proteasome condensate formation in yeast via greater accumulation of polyubiquitinated material available for condensation with proteasomes. My current studies are exploring more deeply the role of the STI1 domain of Dsk2 in proteostasis.