A pathway controlling non-apoptotic developmental cell death engages non-canonical death-promoting activities of the stress factor HSF-1, which, in turn, activates specific components of the ubiquitin-mediated degradation machinery.

Post-translational regulation of retrotransposons plays a key role in preventing retrotransposon mobilization in the epigenetically dynamic mouse germline.

In neurons, inhibition of the proteasome results in feedback inhibition of protein synthesis, mediated by heme-regulated kinase 1, which is optimized to act as both a sensor and an effector.

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.

The 26S proteasome lid subcomplex acts as an external scaffold whose interactions with the ATPase motor stabilize the substrate-engagement-competent state, and control conformational changes upon engagement for subsequent degradation steps.

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 genome-wide screen in yeast reveals that key proteins in ribosome quality control also regulate mutant Huntingtin aggregation and toxicity.

Enhanced proteasomal degradation of TNFAIP3 proteins carrying missense variations is one of the pathophysiological mechanisms underlying HA20.

A comprehensive analysis of yeast mutants has provided clues to understanding the physiological conditions caused by protein overexpression.

KLHL41 acts as a poly-ubiquitin dependent chaperone that prevents the formation of pathogenic nebulin aggregates associated with muscle disease.