Liquid-liquid phase separation (LLPS) has recently emerged as a possible mechanism that enables the localization of ubiquitin (Ub)-binding shuttle proteins to biomolecular condensates to facilitate the degradation of ubiquitinated substrates. Our lab recently showed that the Ub-binding shuttle protein UBQLN2 colocalizes with stress granules in cells and undergoes LLPS in vitro. Specific interactions with monoUb drive disassembly of UBQLN2-rich droplets. On the other hand, we find that polyubiquitin chains of different lengths and linkages can either inhibit or promote UBQLN2 LLPS. Here, I will discuss the complex interplay of interactions among folded domains and intrinsically disordered regions that together mediate LLPS which is further regulated by interactions with polyubiquitin. Using a combination of various spectroscopic and microscopic techniques, our lab aims to dissect how protein quality control mechanisms use LLPS for driving functional outcomes.

Talk by:
Carlos Castañeda
Syracuse University

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