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- W1977521815 abstract "Epithelial cells of the thymus cortex express a unique proteasome particle involved in positive T cell selection. This thymoproteasome contains the recently discovered β5t subunit that has an uncharted activity, if any. We synthesized fluorescent epoxomicin probes that were used in a chemical proteomics approach, entailing activity-based profiling, affinity purification, and LC-MS identification, to demonstrate that the β5t subunit is catalytically active in the murine thymus. A panel of established proteasome inhibitors showed that the broad-spectrum inhibitor epoxomicin blocks the β5t activity and that the subunit-specific antagonists bortezomib and NC005 do not inhibit β5t. We show that β5t has a substrate preference distinct from β5/β5i that might explain how the thymoproteasome generates the MHC class I peptide repertoire needed for positive T cell selection." @default.
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- W1977521815 date "2010-08-01" @default.
- W1977521815 modified "2023-10-16" @default.
- W1977521815 title "Activity-Based Profiling Reveals Reactivity of the Murine Thymoproteasome-Specific Subunit β5t" @default.
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- W1977521815 doi "https://doi.org/10.1016/j.chembiol.2010.05.027" @default.
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