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Protein degradation corrects for imbalanced subunit stoichiometry in OST complex assembly
(2015)Molecular Biology of the CellProtein degradation is essential for cellular homeostasis. We developed a sensitive approach to examining protein degradation rates in Saccharomyces cerevisiae by coupling a SILAC approach to selected reaction monitoring (SRM) mass spectrometry. Combined with genetic tools, this analysis made it possible to study the assembly of the oligosaccharyl transferase complex. The ER-associated degradation machinery compensated for disturbed ...Journal Article -
The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins
(2015)Molecular Biology of the CellMisfolded proteins of the secretory pathway are extracted from the endoplasmic reticulum (ER), polyubiquitylated by a protein complex termed the Hmg-CoA reductase degradation ligase (HRD-ligase), and degraded by cytosolic 26S proteasomes. This process is termed ER-associated protein degradation (ERAD). We previously showed that the membrane protein Der1, which is a subunit of the HRD-ligase, is involved in the export of aberrant polypeptides ...Journal Article -
Distinct donor and acceptor specificities of Trypanosoma brucei oligosaccharyltransferases
(2009)The EMBO JournalJournal Article -
Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum
(2009)The Journal of Cell BiologyTo maintain protein homeostasis in secretory compartments, eukaryotic cells harbor a quality control system that monitors protein folding and protein complex assembly in the endoplasmic reticulum (ER). Proteins that do not fold properly or integrate into cognate complexes are degraded by ER-associated degradation (ERAD) involving retrotranslocation to the cytoplasm and proteasomal peptide hydrolysis. N-linked glycans are essential in ...Journal Article