Akt can regulate the ubiquitin-proteasome system by mediating phosphorylation and activation of USP14, which may have implications in the control of global proteostasis by growth factors and in tumorigenesis.

Through interactions with both ubiquitin units that emanate from a branch point in polyubiquitin, UCH37 recognizes and hydrolyzes branched chains to promote proteasome-mediated degradation upon proteolytic stresses.

Aberrant neddylation of non-cullin substrates disrupts normal cell cycle progression.

A ubiquitin E3 ligase localizes to focal adhesions at the front of migrating human cells where it regulates cytoskeletal dynamics by targeting a focal adhesion protein.

Genetic mapping reveals widespread, complex genetic effects on protein degradation by the ubiquitin-proteasome system, the primary protein degradation pathway in eukaryotic cells.

Endoproteolytic cleavage of the ribosomal precursor protein FUBI-eS30 is required for efficient maturation of small ribosomal subunits in the cytoplasm of human cells and involves the nucleolar deubiquitinase USP36.

Chemical perturbation-dependent deep mutational scanning data collected by a lab-based interdisciplinary graduate class resolves a paradox between the high evolution conservation and the high mutational tolerance of the protein ubiquitin.

A combination of spatial proteomic and autophagic flux approaches was used to reveal the landscape of turnover of damaged lysosomes, demonstrating a key role for the autophagy receptor TAX1BP1 and its associated kinase TBK1 in both HeLa cells and iNeurons.

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.

The proteasomal deubiquitinase UCHL5/UCH37 uses a face distinct from the canonical ubiquitin binding site to engage K48-linked ubiquitin chains and catalyze chain debranching.