Secretory and membrane proteins are co-translationallytranslocated into the lumen of the endoplasmic reticulum (ER), where theyattain their correct three-dimensional structure. The high flux of proteinsthrough the ER leads to terminal misfolding of a subset of foldingintermediates. The nature of oligosaccharides, cotranslationally attached tothe amide side chains of asparagines residues, play pivotal role in decisionmaking process during the protein degradation. While properly foldedglycoproteins are further exported to the Golgi, terminally misfolded proteinsare removed from the ER lumen in a process collectively described as ER-associateddegradation (ERAD). The mechanisms that the ER employs to distinguishterminally misfolded glycoproteins from folding intermediates is the centralquestion in the field of protein degradation in the ER. Studies in S. cerevisiae demonstrated essential roles of several carbohydrate-recognizing proteins in ERAD. By their in vitro characterization, we aim to define molecular logic of substrate recognition in ERAD.

Defining roles on N-Glycans in endoplasmic reticulum-mediated quality control

239th National Meeting (2010)

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