Biophysical experiments, pulse-chase assays, and molecular dynamics simulations reveal how the proteasome targeting signal Fat10 can modulate the structure of substrate proteins to potentially regulate their degradation by the proteasome.

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.

Novel post-translational modification of pattern recognition receptor TLR2 has consequences in bacterial infection and inflammatory signaling.

The poorly characterized BTB-protein SPOPL is required to maintain the function of the late endosomal system and the endocytic adaptor EPS15 is therein targeted by the SPOPL/Cullin-3 ubiquitin ligase complex for degradation.

Stimulation of cells with a mitochondria-depolarizing mitogen reveals a requirement for UBQLN1 expression in maintaining protein synthesis levels during cell cycle entry.

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 novel ALS-associated variant in UBQLN4 impairs proteasome function and beta-catenin degradation to drive aberrant axon morphogenesis in motor neurons.

Temperature-sensitive mitochondrial outer membrane proteins used as novel quality control substrates reveal a unique mitochondria-associated degradation pathway consisting of both cytosolic and mitochondrial ubiquitin-proteasome system machinery.

Divergence in immunoproteasome substrate specificity and regulation from the constitutive proteasome impacts peptide cleavage quantity and the cellular capacity of the ubiquitin-proteasome system.

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.