Maintenance of ubiquitin homeostasis is essential for proper control of the size of postsynaptic density and the growth of specialized membrane structure.

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.

The structure of Bre1’s Rad6-binding domain in complex with Rad6 provides insights into the Bre1 and Rad6-catalyzed histone protein H2B mono-ubiquitination.

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.

Rqc2-mediated modification of ribosome-stalled nascent chains with "CAT tails" promotes formation of insoluble aggregates suggesting that proteins can become specifically marked for aggregation.

Lys63-linked diubiquitin exists as an ensemble of conformational states, each responsible for binding to a target protein through conformational selection.

The E3 ubiquitin ligase complex linear ubiquitin chain assembly complex (LUBAC) forms a branched chain on linear ubiquitin chains depending on the RING-in-between-RING-type E3 ligase heme-oxidized IRP2 ubiquitin ligase 1 (HOIL-1L).

UBX proteins reduce the ubiquitin threshold of mammalian p97-UFD1-NPL4.

Expression of plant immune genes is controlled by the opposing actions of ubiquitin ligases and deubiquitinases that modify the master coactivator NPR1, thereby regulating its intrinsic transcriptional activity.

A cell-free system combined with cell-based assays elucidate the biochemical mechanism of signal transduction mediated by the mitochondrial protein MAVS and delineates the role of ubiquitin E3 ligases in antiviral innate immune responses.