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.

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.

In fruit flies, maternally deposited RNA-binding proteins are removed during the maternal-to-zygotic transition via a mechanism of translational upregulation of Kondo, the key E2 enzyme, at egg activation.

DDB1, a component of the ubiquitin proteasome system, plays a role in both hematopoietic and embryonic stem cell self-renewal and differentiation.

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.

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.

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.

Faithful models of RMC require SMARCB1 loss for survival, and genetic and small-molecule screens identify inhibition of the ubiquitin-proteasome system (UPS) as a potential therapeutic approach for SMARCB1 deficient cancers.

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

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