作者: Christopher M Cabral , Yan Liu , Richard N Sifers
DOI: 10.1016/S0968-0004(01)01942-9
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摘要: In the early secretory pathway, asparagine-linked glycosylation facilitates conformational maturation of diverse polypeptides by promoting their physical engagement with glycoprotein-folding machinery. Misfolded glycoproteins are selectively eliminated from endoplasmic reticulum a stringent process conformation-based quality control. Recent studies indicate that small ensemble oligosaccharide-processing enzymes and lectins use appendage to orchestrate selective disposal numerous transport-defective pathway. The glycan-based system functions as an evolutionarily conserved terminal checkpoint in eukaryote genome expression. That mechanisms which glycoprotein substrates recruited for degradation diverge at level signal recognition reflects previously unappreciated component cellular differentiation higher eukaryotes.