Metabolic labelling reveals complex proteome dynamics in tendon, with faster turnover of proteins in the glycoprotein-rich interfascicular matrix compared to the collagen-rich fascicular matrix.
Within the isolated lid sub-complex of the proteasome, a finely tuned network of interactions maintains the deubiquitinase in an inhibited conformation; dramatic rearrangements of the lid subunits upon incorporation into the holoenzyme lead to the deubiquitinase’s activation.
Structures of active and inactive conformations of a PP2C family phosphatase reveal a conserved switch that controls enzymatic activity and point to an unexpected relationship between phosphatases and proteasomal proteases.
Faithful models of RMC require SMARCB1 loss for survival, and genetic and small-molecule screens identify inhibition of the ubiquitin-proteasome system (UPS) as a potential therapeutic approach for SMARCB1 deficient cancers.
Structural and biochemical characterization of the protease domain of an ABC transporter demonstrates the basis for recognition of substrate leader peptides.
Proteases from diverse viruses, the first described pathogen-encoded activators of human NLRP1, cleave NLRP1 at a sequence that mimics the viral polyprotein, resulting in inflammasome activation and pro-inflammatory cytokine release.
Analysis of genome integrity in primary murine B-cells reveals how depleting 26S proteasome activity enhanced cell survival following treatment with topoisomerase poisons.
Reducing the expression of 19S subunits shifts the ratio of 20S/26S proteasome complexes and provides a powerful survival advantage in the face of lethal proteasome inhibition.
