http://purl.uniprot.org/citations/26644575 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/26644575 | http://www.w3.org/2000/01/rdf-schema#comment | "Dynamic cycling of N-Acetylglucosamine (GlcNAc) on serine and threonine residues (O-GlcNAcylation) is an essential process in all eukaryotic cells except yeast, including Saccharomyces cerevisiae and Schizosaccharomyces pombe. O-GlcNAcylation modulates signaling and cellular processes in an intricate interplay with protein phosphorylation and serves as a key sensor of nutrients by linking the hexosamine biosynthetic pathway to cellular signaling. A longstanding conundrum has been how yeast survives without O-GlcNAcylation in light of its similar phosphorylation signaling system. We previously developed a sensitive lectin enrichment and mass spectrometry workflow for identification of the human O-linked mannose (O-Man) glycoproteome and used this to identify a pleothora of O-Man glycoproteins in human cell lines including the large family of cadherins and protocadherins. Here, we applied the workflow to yeast with the aim to characterize the yeast O-Man glycoproteome, and in doing so, we discovered hitherto unknown O-Man glycosites on nuclear, cytoplasmic, and mitochondrial proteins in S. cerevisiae and S. pombe. Such O-Man glycoproteins were not found in our analysis of human cell lines. However, the type of yeast O-Man nucleocytoplasmic proteins and the localization of identified O-Man residues mirror that of the O-GlcNAc glycoproteome found in other eukaryotic cells, indicating that the two different types of O-glycosylations serve the same important biological functions. The discovery opens for exploration of the enzymatic machinery that is predicted to regulate the nucleocytoplasmic O-Man glycosylations. It is likely that manipulation of this type of O-Man glycosylation will have wide applications for yeast bioprocessing."xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1511743112"xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/author | "Neubert P."xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/author | "Petersen B.L."xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/author | "Halim A."xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/author | "Clausen H."xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/author | "Vakhrushev S.Y."xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/author | "Strahl S."xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/author | "Joshi H.J."xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/author | "Larsen I.S."xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/pages | "15648-15653"xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/title | "Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast."xsd:string |
http://purl.uniprot.org/citations/26644575 | http://purl.uniprot.org/core/volume | "112"xsd:string |
http://purl.uniprot.org/citations/26644575 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26644575 |
http://purl.uniprot.org/citations/26644575 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/26644575 |
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