Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and 
a candidate player in the early steps of protein N-glycosylation

Schallus, Thomas; Jaeckh, Christine; Feher, Krisztina; Palma, Angelina S.; Liu, Yuhong; Simpson, Jeremy C.; Mackeen, Mukram; Stier, Gunter; Gibson, Toby J.; Feizi, Ten; Pieler, Tomas; Muhle-Goll, Claudia

doi:10.1091/mbc.E08-04-0354

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Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation

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Schallus, Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Feher, Krisztina
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Liu, Yuhong
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Stier, Gunter
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Muhle-Goll, Claudia
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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http://www.molbiolcell.org/content/19/8/3404.full.pdf+html
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http://www.molbiolcell.org/content/suppl/2008/06/04/E08-04-0354.DC1/schallus_et_al_supplement.pdf
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Citation

Schallus, T., Jaeckh, C., Feher, K., Palma, A. S., Liu, Y., Simpson, J. C., et al. (2008). Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation. Molecular Biology of the Cell, 19(8), 3404-3414. doi:10.1091/mbc.E08-04-0354.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002E-8C42-6

Abstract

N-Glycosylation starts in the endoplasmic reticulum (ER) where a 14-sugar glycan composed of three glucoses, nine mannoses, and two N-acetylglucosamines (Glc(3)Man(9)GlcNAc(2)) is transferred to nascent proteins. The glucoses are sequentially trimmed by ER-resident glucosidases. The Glc(3)Man(9)GlcNAc(2) moiety is the substrate for oligosaccharyltransferase; the Glc(1)Man(9)GlcNAc(2) and Man(9)GlcNAc(2) intermediates are signals for glycoprotein folding and quality control in the calnexin/calreticulin cycle. Here, we report a novel membrane-anchored ER protein that is highly conserved in animals and that recognizes the Glc(2)-N-glycan. Structure determination by nuclear magnetic resonance showed that its luminal part is a carbohydrate binding domain that recognizes glucose oligomers. Carbohydrate microarray analyses revealed a uniquely selective binding to a Glc(2)-N-glycan probe. The localization, structure, and binding specificity of this protein, which we have named malectin, open the way to studies of its role in the genesis, processing and secretion of N-glycosylated proteins.