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

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

Research output: Contribution to journalArticle

159 Citations (Scopus)

Abstract

N-Glycosylation starts in the endoplasmic reticulum (ER) where a 14-sugar glycan composed of three glucoses, nine mannoses, and two N-acetylglucosamines (Glc3Man9GlcNAc2) is transferred to nascent proteins. The glucoses are sequentially trimmed by ER-resident glucosidases. The Glc3Man9GlcNAc2 moiety is the substrate for oligosaccharyl-transferase; the Glc1Man9GlcNAc2 and Man9GlcNAc2 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 Glc2-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.

Original languageEnglish
Pages (from-to)3404-3414
Number of pages11
JournalMolecular Biology of the Cell
Volume19
Issue number8
DOIs
Publication statusPublished - Aug 2008
Externally publishedYes

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Glycosylation
Endoplasmic Reticulum
Polysaccharides
Glucose
Calnexin
Carbohydrates
Calreticulin
Glucosidases
Proteins
Acetylglucosamine
Microarray Analysis
Transferases
Quality Control
Glycoproteins
Carrier Proteins
Magnetic Resonance Spectroscopy
Membranes
saccharide-binding proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

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; Fehér, Krisztina; Palma, Angelina S.; Liu, Yan; Simpson, Jeremy C.; Mohamed Mackeen, Muhammad Mukram; Stier, Gunter; Gibson, Toby J.; Feizi, Ten; Pieler, Tomas; Muhle-Goll, Claudia.

In: Molecular Biology of the Cell, Vol. 19, No. 8, 08.2008, p. 3404-3414.

Research output: Contribution to journalArticle

Schallus, T, Jaeckh, C, Fehér, K, Palma, AS, Liu, Y, Simpson, JC, Mohamed Mackeen, MM, Stier, G, Gibson, TJ, Feizi, T, Pieler, T & Muhle-Goll, C 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, vol. 19, no. 8, pp. 3404-3414. https://doi.org/10.1091/mbc.E08-04-0354
Schallus, Thomas ; Jaeckh, Christine ; Fehér, Krisztina ; Palma, Angelina S. ; Liu, Yan ; Simpson, Jeremy C. ; Mohamed Mackeen, Muhammad Mukram ; Stier, Gunter ; Gibson, Toby J. ; Feizi, Ten ; Pieler, Tomas ; Muhle-Goll, Claudia. / Malectin : A novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation. In: Molecular Biology of the Cell. 2008 ; Vol. 19, No. 8. pp. 3404-3414.
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