Lipid-linked oligosaccharide biosynthesis (Saccharomyces cerevisiae)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="Lipid-Linked Oligosaccharide Biosynthesis" Organism="Saccharomyces cerevisiae"> <Comment Source="GenMAPP remarks">Based on http://pathway.yeastgenome.org/biocyc/</Comment> <Comment Source="WikiPathways-category">Metabolic Process</Comment> <Comment Source="WikiPathways-description">In eukaryotes, N-linked (asparagine-linked) glycosylation is the most common form of protein modification of secretory and membrane proteins, and is involved in a variety of cellular processes, such as protein folding, sorting and stability (reviewed in (CITS: [15189166][8472892][3896128])). The initial steps of N-linked glycosylation, which are also known as the dolichol pathway of N-linked glycosylation, and lipid- and dolichol-linked oligosaccharide biosynthesis, involve the synthesis of a core oligosaccharide (glucosyl)&lt;sub&gt;3&lt;/sub&gt;(mannosyl)&lt;sub&gt;9&lt;/sub&gt;(N-acetylglucosamine)&lt;sub&gt;2&lt;/sub&gt;, abbreviated, Glc&lt;sub&gt;3&lt;/sub&gt;Man&lt;sub&gt;9&lt;/sub&gt;GlcNAc&lt;sub&gt;2&lt;/sub&gt;, on the lipid carrier, dolichol-pyrophosphate (Dol-PP) (reviewed in (CITS: [9878760][8472892][3896128])). The ordered assembly of the core oligosaccharide is highly conserved throughout eukaryotic evolution. The assembly starts on the cytoplasmic side of the endoplasmic reticulum (ER), where N-acetylglucosamine-1-phosphate (GlcNAc-1-phosphate) is transferred from uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc) to dolichol-phosphate (Dol-P) followed by the addition of one N-acetylglucosamine (GlcNAc) and five mannose residues from UDP-GlcNAc and guanosine 5'-diphosphomannose (GDP-Man), respectively. The resulting lipid-linked precursor (Man&lt;sub&gt;5&lt;/sub&gt;GlcNAc&lt;sub&gt;2&lt;/sub&gt;-PP-Dol) is translocated "flipped" into the lumen of the ER by a flippase, which which is endoded by &lt;i&gt;RFT1&lt;/i&gt; in &lt;i&gt;S. cerevisiae&lt;/i&gt;. Once in the lumen, the oligosaccharide is extended by four mannose and three glucose residues derived from dolichyl-phosphate-mannose (Dol-P-Man) and dolichyl-phosphate-glucose (Dol-P-Glc), respectively. The enzyme complex oligosaccharyltransferase (OST) transfers the preassembled oligosaccharide, Glc&lt;sub&gt;3&lt;/sub&gt;Man&lt;sub&gt;9&lt;/sub&gt;GlcNAc&lt;sub&gt;2&lt;/sub&gt;, from the lipid carrier Dol-PP to selected asparagine residues of nascent polypeptides as the polypeptides pass into the lumen of the ER (CITS: [11580295])(CITS: [9405463]). Once attached to the protein, the N-linked oligosaccharide is further modified by a series of trimming and elongation reactions beginning in the ER and ending in the late Golgi compartment (CITS: [8054711]). In the ER, the oligosaccharide is trimmed of its 3 glucose residues and a specific mannose residue to form Man&lt;sub&gt;8&lt;/sub&gt;GlcNAc&lt;sub&gt;2&lt;/sub&gt;. The glucose residues are removed by glucosidases I and II, and in &lt;i&gt;S. cerevisiae&lt;/i&gt; the mannose is removed by the alpha-1,2-mannosidase Mns1p, which is part of the editing mechanism that promotes the exit of correctly folded glycoproteins from the ER (CITS: [9732283]). Once the four monosaccharides are removed, the glycoproteins are transported from the ER to the Golgi, where the yeast and mammalian pathways diverge (CITS: [3304149]). The lipid-linked oligosaccharide biosynthetic pathway is of particular interest in humans, because defects in the glycosyltransferases involved lead to congenital disorders of glycosylation (CITS: [11306275][17024709]). 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rdf:datatype="http://www.w3.org/2001/XMLSchema#string">11278778</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">The yeast ALG11 gene specifies addition of the terminal alpha 1,2-Man to the Man5GlcNAc2-PP-dolichol N-glycosylation intermediate formed on the cytosolic side of the endoplasmic reticulum.</bp:TITLE> <bp:SOURCE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">J Biol Chem</bp:SOURCE> <bp:YEAR rdf:datatype="http://www.w3.org/2001/XMLSchema#string">2001</bp:YEAR> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Cipollo JF</bp:AUTHORS> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Trimble RB</bp:AUTHORS> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Chi JH</bp:AUTHORS> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Yan Q</bp:AUTHORS> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Dean N</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" rdf:id="jyg"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">9878760</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">The dolichol pathway of N-linked glycosylation.</bp:TITLE> <bp:SOURCE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Biochim Biophys Acta</bp:SOURCE> <bp:YEAR rdf:datatype="http://www.w3.org/2001/XMLSchema#string">1999</bp:YEAR> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Burda P</bp:AUTHORS> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Aebi M</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" rdf:id="o7c"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">10336995</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases.</bp:TITLE> <bp:SOURCE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Glycobiology</bp:SOURCE> <bp:YEAR rdf:datatype="http://www.w3.org/2001/XMLSchema#string">1999</bp:YEAR> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Burda P</bp:AUTHORS> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Jakob CA</bp:AUTHORS> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Beinhauer J</bp:AUTHORS> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Hegemann JH</bp:AUTHORS> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Aebi M</bp:AUTHORS> </bp:PublicationXref> <bp:openControlledVocabulary xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#"><bp:TERM>lipid metabolic pathway</bp:TERM><bp:ID>PW:0000010</bp:ID><bp:Ontology>Pathway Ontology</bp:Ontology></bp:openControlledVocabulary></Biopax> </Pathway>

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