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Nat Chem Biol. 2007 Jun;3(6):313-20.

N-glycan structure dictates extension of protein folding or onset of disposal.

Author information

1
Institute for Research in Biomedicine, Via V. Vela 6, CH-6500 Bellinzona, Switzerland. maurizio.molinari@irb.unisi.ch

Abstract

The endoplasmic reticulum (ER) is the site of folding for proteins that are resident in the ER or that are destined for the Golgi, endosomes, lysosomes, the plasma membrane, or secretion. Cotranslational addition of preassembled glucose(3)-mannose(9)-N-acetylglucosamine(2) core oligosaccharides (N-glycosylation) is a common event for polypeptides synthesized in this compartment. Protein-bound oligosaccharides are exposed to several ER glycanases that sequentially remove terminal glucose or mannose residues. Their activity must be tightly regulated because the N-glycan composition determines whether the associated protein is subjected to folding attempts in the ER lumen or whether it is retrotranslocated into the cytosol and degraded.

PMID:
17510649
DOI:
10.1038/nchembio880
[Indexed for MEDLINE]

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