Calnexin can interact with N-linked glycans located close to the endoplasmic reticulum membrane

FEBS Letters
H AnderssonG von Heijne

Abstract

Calnexin is a central component of the 'quality control' system in the endoplasmic reticulum (ER). Calnexin binds to monoglycosylated oligosaccharides on incompletely folded soluble and membrane proteins in the lumen of the ER and prevents exit from the organelle. We have previously found that the oligosaccharide transferase enzyme can add glycosyl moieties to a membrane protein when the acceptor site is as close as 12-13 residues away from the nearest transmembrane segment (J. Biol. Chem. 268, 5798). We now show that calnexin can bind to oligosaccharides located this close to the membrane, suggesting that its binding site is held at a similar distance from the membrane as is the active site of the oligosaccharide transferase. We further show that calnexin can bind efficiently to glycosylated but not to non-glycosylated forms of a bacterial inner membrane protein, suggesting that it does not have a general affinity for non-glycosylated proteins.

References

Dec 1, 1991·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·A D Elbein
Dec 1, 1991·Molecular Microbiology·R E Dalbey
Mar 1, 1994·Trends in Biochemical Sciences·J J BergeronD B Williams
Feb 1, 1994·Proceedings of the National Academy of Sciences of the United States of America·C HammondA Helenius
Jun 14, 1996·The Journal of Biological Chemistry·K S CannonA Helenius

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Citations

Dec 20, 2005·The Journal of Biological Chemistry·Qiuming GongZhengfeng Zhou
Oct 12, 2007·Physiological Reviews·Daniel N Hebert, Maurizio Molinari
Apr 25, 2000·The Journal of Biological Chemistry·U G DanilczykD B Williams

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