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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

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002E-8C42-6 Version Permalink: https://hdl.handle.net/21.11116/0000-0000-E3B9-F
Genre: Journal Article

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 Creators:
Schallus, Thomas1, Author           
Jaeckh, Christine, Author
Feher, Krisztina1, Author           
Palma, Angelina S., Author
Liu, Yuhong2, Author           
Simpson, Jeremy C., Author
Mackeen, Mukram, Author
Stier, Gunter1, Author           
Gibson, Toby J., Author
Feizi, Ten, Author
Pieler, Tomas, Author
Muhle-Goll, Claudia1, Author           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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 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.

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Language(s): eng - English
 Dates: 2008-04-062008-05-282008-06-042008-08-01
 Publication Status: Issued
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1091/mbc.E08-04-0354
URI: http://www.ncbi.nlm.nih.gov/pubmed/18524852
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Title: Molecular Biology of the Cell
  Other : Mol. Biol. Cell
Source Genre: Journal
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Publ. Info: American Society for Cell Biology
Pages: - Volume / Issue: 19 (8) Sequence Number: - Start / End Page: 3404 - 3414 Identifier: ISSN: 1059-1524
CoNE: https://pure.mpg.de/cone/journals/resource/954927716372_1