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Glycosylation is an essential step in the synthesis of complex carbohydrates in eukaryotes. N-linked glycosylation is an important type of protein modification, which is initiated by the formation of an oligosaccharyl-diphosphate on a conserved asparagine residue within the consensus sequence Asn-Xaa-Ser/Thr (NXS/T). Several studies of N-linked glycosylation have shown that the N-oligosaccharyl-diphosphate-transferase (OT) and the saccharide-specific-oligosaccharyltransferase (OST) are responsible for the first and second steps, respectively, of this process. However, the function of the subsequently acting enzymes has not been elucidated. We identified SGL1 (syntaxin 11) as a gene involved in the biosynthesis of N-linked glycans, and demonstrated that SGL1 is a component of the membrane-bound protein complex required for the transport of nascent glycoprotein precursors to the Golgi apparatus. Here, we show that the SGL1 protein is localized in the Golgi apparatus and mediates the Golgi apparatus-endoplasmic reticulum transport of N-acetylglucosaminyltransferase I (GlcNAcT-I). Our results provide evidence for the importance of the intracellular localization of GlcNAcT-I in N-linked glycosylation. there are no source
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