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A critical component of the cellular response to unfolded proteins is the widespread rescue of ribosomes that stall on endonucleolytically-cleaved mRNA transcripts.

Transcriptomic and genetic analyses of FoxO target genes reveal a key function of ER-associated protein degradation in growth regulation of Tsc1-deficient tissues.

Novel disease pathways underlie disease pathogenesis in Kelch-related nemaline myopathy through proteomic remodeling.

The cytoplasmic enzyme N-glycanase 1 plays an evolutionary conserved role in promoting the ERAD-mediated retrotranslocation of misfolded Dpp/BMP4 from the ER, thereby allowing BMP signaling in specific contexts.

A generalizable approach to identify sequence features driving degradation from the endoplasmic reticulum (ER) provides useful tools for enabling ER-localized protein degradation.

Dendritic cell recognition and processing of antigens from dead cells, utilising the Clec9A-damage recognition receptor, is controlled by a novel RNF41-ubiquitin-mediated regulatory pathway.

Ubiquitin ligase adaptors target the selective clearance of misfolded plasma membrane proteins.

Biochemical analysis reveals the entire route of oligosaccharide processing from M9 to M8B and then to oligosaccharides exposing the α1,6-linked mannosyl residue (M7A, M6, and M5), and the enzymes (EDEM2 and EDEM3/1) responsible for endoplasmic reticulum-associated degradation of misfolded glycoproteins.

Alternative splicing and the endoplasmic reticulum (ER)-associated protein degradation (ERAD) system represent essential, fat depot-specific components of the adipogenesis that are altered in preadipocytes from obese individuals with metabolic disease.

Parallel branches of the ERAD pathway regulate sterol synthesis at multiple steps via feedback inhibition.