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Ubiquitin proteasome system in immune regulation and therapeutics

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ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.coph.2022.102310

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  1. National Institutes of Health [R35 GM137452]

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This article summarizes the role of the ubiquitin proteasome system (UPS) and E3 ligases in immune-related diseases. It discusses the involvement of deregulated E3 ligases/UPS components in lymphomas, neurodevelopmental abnormalities, and cancers. The article also highlights the potential of targeting E3 ligases for therapeutic intervention.
The ubiquitin proteasome system (UPS) is a proteolytic machinery for the degradation of protein substrates that are post-translationally conjugated with ubiquitin polymers through the enzymatic action of ubiquitin ligases, in a process termed ubiquitylation. Ubiquitylation of substrates precedes their proteolysis via proteasomes, a hierarchical feature of UPS. E3-ubiquitin ligases recruit protein substrates providing specificity for ubiquitylation. Innate and adaptive immune system networks are regulated by ubiquitylation and substrate degradation via E3-ligases/UPS. Deregulation of E3-ligases/UPS components in immune cells is involved in the development of lymphomas, neurodevelopmental abnormalities, and cancers. Targeting E3-ligases for therapeutic intervention provides opportunities to mitigate the unintended broad effects of 26S proteasome inhibition. Recently, bifunctional moieties such as PROTACs and molecular glues have been developed to re-purpose E3-ligases for targeted degradation of unwanted aberrant proteins, with a potential for clinical use. Here, we summarize the involvement of E3ligases/UPS components in immune-related diseases with perspectives.

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