Dissecting glycoprotein quality control in the secretory pathway

In the early secretory pathway, asparagine-linked glycosylation facilitates the conformational maturation of diverse polypeptides by promoting their physical engagement with the glycoprotein-folding machinery. Misfolded glycoproteins are selectively eliminated from the endoplasmic reticulum by a str...

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Bibliographic Details
Published in:Trends in Biochemical Sciences 2001-10, Vol.26 (10), p.619-624
Main Authors: Cabral, Christopher M, Liu, Yan, Sifers, Richard N
Format: Article
Language:English
Subjects:
Animals
Asparagine - chemistry
Calcium-Binding Proteins - metabolism
Calnexin
Calreticulin
Carbohydrate Sequence
Endoplasmic Reticulum - metabolism
glycoprotein
Glycoproteins - chemistry
Glycoproteins - metabolism
Glycosylation
Mannosidases - metabolism
misfolded protein
Molecular Sequence Data
oligosaccharide-processing enzyme
protein degradation
Protein Folding
protein secretion
Quality Control
Ribonucleoproteins - metabolism
Signal Transduction
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Summary:In the early secretory pathway, asparagine-linked glycosylation facilitates the conformational maturation of diverse polypeptides by promoting their physical engagement with the glycoprotein-folding machinery. Misfolded glycoproteins are selectively eliminated from the endoplasmic reticulum by a stringent process of conformation-based quality control. Recent studies indicate that a small ensemble of oligosaccharide-processing enzymes and lectins use the asparagine-linked appendage to orchestrate the selective disposal of numerous transport-defective glycoproteins from the early secretory pathway. The glycan-based disposal system functions as an evolutionarily conserved terminal checkpoint in eukaryote genome expression. That the mechanisms by which glycoprotein substrates are recruited for degradation diverge at the level of signal recognition reflects a previously unappreciated component of cellular differentiation in higher eukaryotes.
ISSN:0968-0004
1362-4326
DOI:10.1016/S0968-0004(01)01942-9