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

@article{citeulike:5347727, 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.}, author = {Schallus, Thomas and Jaeckh, Christine and Feh\'{e}r, Krisztina and Palma, Angelina S. and Liu, Yan and Simpson, Jeremy C. and Mackeen, Mukram and Stier, Gunter and Gibson, Toby J. and Feizi, Ten and Pieler, Tomas and Muhle-Goll, Claudia}, citeulike-article-id = {5347727}, citeulike-linkout-0 = {http://dx.doi.org/10.1091/mbc.E08-04-0354}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18524852}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18524852}, doi = {10.1091/mbc.E08-04-0354}, issn = {1939-4586}, journal = {Molecular biology of the cell}, keywords = {er, glyco, glycosidase, lectin}, month = {August}, number = {8}, pages = {3404--3414}, posted-at = {2009-08-04 08:54:37}, priority = {2}, title = {Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation.}, url = {http://dx.doi.org/10.1091/mbc.E08-04-0354}, volume = {19}, year = {2008} }

TY - JOUR ID - citeulike:5347727 L3 - citeulike-article-id:5347727 N2 - 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. IS - 8 JF - Molecular biology of the cell SN - 1939-4586 EP - 3414 TI - Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation. VL - 19 SP - 3404 KW - er KW - glyco KW - glycosidase KW - lectin AU - Schallus, Thomas AU - Jaeckh, Christine AU - Fehér, Krisztina AU - Palma, Angelina AU - Liu, Yan AU - Simpson, Jeremy AU - Mackeen, Mukram AU - Stier, Gunter AU - Gibson, Toby AU - Feizi, Ten AU - Pieler, Tomas AU - Muhle-Goll, Claudia PY - 2008/08// UR - http://dx.doi.org/10.1091/mbc.E08-04-0354 ER -