ユビキチン・プロテアソーム相分離による多彩な細胞内機能

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  • Co-condensates of ubiquitin and proteasome play diverse roles in cellular functions

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<p>The ubiquitin-proteasome system (UPS) plays an essential role in maintaining proteostasis by selective degradation of aberrant proteins. Ubiquitin inclusion is a hallmark of almost all neurodegenerative diseases, thereby suggesting that dysfunction of the UPS leads to neurodegenerative diseases. Recently, ubiquitin-dependent phase separation and transition have been implicated in disease pathogenesis, but little is known about the molecular mechanisms involved. We previously found that the nuclear proteasomes undergo liquid-liquid phase separation (LLPS) with ubiquitylated substrates upon hyperosmotic stress, forming proteolytic droplets. Furthermore, we have found that various stresses induce the formation of distinct co-condensates of ubiquitin and proteasomes, suggesting that their co-condensation is the universal cellular response machinery. Unexpectedly, some of the co-condensates are unlikely proteolytic droplets. They exhibit the hydrogel-like properties and potentially non-proteolytic functions. Here, we present and discuss the current perspectives on the co-condensation of ubiquitin and proteasome.</p>

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