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XB-ART-38618
Mol Biol Cell August 1, 2008; 19 (8): 3404-14.

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 , Fehér K , Palma AS , Liu Y , Simpson JC , Mackeen M , Stier G , Gibson TJ , Feizi T , Pieler T , Muhle-Goll C .


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.

PubMed ID: 18524852
PMC ID: PMC2488313
Article link: Mol Biol Cell
Grant support: [+]
Genes referenced: acta4 canx man1a1 mlec pdia2 sult2a1 txk


Article Images: [+] show captions
References [+] :
Afelik, Pancreatic protein disulfide isomerase (XPDIp) is an early marker for the exocrine lineage of the developing pancreas in Xenopus laevis embryos. 2003, Pubmed, Xenbase


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