Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für medizinische Forschung     Collection: Abteilung Zellphysiologie     Display Documents



ID: 566002.0, MPI für medizinische Forschung / Abteilung Zellphysiologie
Malectin: a novel carbohydrate−binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N−glycosylation
Translation of Title:Malectin: a novel carbohydrate−binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N−glycosylation
Authors:Schallus, Thomas; Jaeckh, Christine; Fehér, Krisztina; Palma, Angelina S.; Liu, Yuhong; Simpson, Jeremy C.; Mackeen, Mukram; Stier, Gunter; Gibson, Toby J.; Feizi, Ten; Pieler, Tomas; Muhle−Goll, Claudia
Language:English
Date of Publication (YYYY-MM-DD):2008-08-01
Title of Journal:Molecular Biology of the Cell
Journal Abbrev.:Mol. Biol. Cell
Volume:19
Issue / Number:8
Start Page:3404
End Page:3414
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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
Last Change of the Resource (YYYY-MM-DD):--
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Abteilung Zellphysiologie
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
External Affiliations:European Molecular Biology Laboratory, 69117 Heidelberg, Germany; Department of Developmental Biochemistry und University Medical Center Göttingen, 37077 Göttingen, Germany; The Glycosciences Laboratory, Faculty of Medicine, Imperial College London, Northwick Park and St. Mark's Hospital Campus, Harrow, Middlesex HA1 3UJ, United Kingdom; Oxford Glycobiology Institute, University of Oxford, Oxford OX1 3QU, United Kingdom
Identifiers:LOCALID:7258
URI:http%3A%2F%2Fwww.molbiolcell.org%2Fcgi%2Freprint%2...
URI:http%3A%2F%2Fwww.molbiolcell.org%2Fcgi%2Fcontent%2...
URI:http%3A%2F%2Fwww.molbiolcell.org%2Fcgi%2Fcontent%2...
DOI:%2010.1091%2Fmbc.E08-04-0354
Full Text:
Sorry, no privileges
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.