Cereblon-based small-molecule degraders rely on the sequential action of ubiquitin-conjugating enzymes UBE2G1 and UBE2D3 to assemble K48-linked polyubiquitin chains on cereblon neomorphic substrates, resulting in their proteasomal degradation.

Human cullin-RING ligases are buffered to a much greater extent than had been previously appreciated, and the roles of ubiquitin chain extension enzymes are far more nuanced at physiological concentrations.

Interacting MKS1 and UBE2E1 regulate canonical Wnt signaling through modulation of beta-catenin levels at the base of primary cilium, providing new insights into ciliopathy disease mechanisms.

Erythroid maturation-dependent remodelling of CTLH E3 complex, along with its cognate E2, controls the orderly progression of human erythropoiesis, thus establishing a paradigm for other E2-E3 ubiquitylation modules involved in developmental processes.

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.

Phosphorylation deactivates TRIM21 B Box autoinhibition to licence proinflammatory signalling by cytosolic antibodies.

The HIV-1 Tat protein hijacks host non-degradative ubiquitination to trigger the nuclear import of the transcription elongation factor, P-TEFb.

Emerin, a protein that plays key roles in nuclear organization, can be dynamically degraded in response to environmental stimuli such as ER stress.

Proteomic, biochemical and cell-based analyses of the heterodecameric core GID/CTLH E3 ligase complex reveal its molecular architecture, activity determinants, and function in targeting the tumor suppressor Hbp1 and other substrates required for cell proliferation.