Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast
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 intricat...
Gespeichert in:
| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
October 12, 2015
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| In: |
Proceedings of the National Academy of Sciences of the United States of America
Year: 2015, Jahrgang: 112, Heft: 51, Pages: 15648-15653 |
| ISSN: | 1091-6490 |
| DOI: | 10.1073/pnas.1511743112 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.1073/pnas.1511743112 Verlag, Volltext: http://www.pnas.org/content/112/51/15648 
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| Verfasserangaben: | Adnan Halim, Ida Signe Bohse Larsen, Patrick Neubert, Hiren Jitendra Joshi, Bent Larsen Petersen, Sergey Y. Vakhrushev, Sabine Strahl, and Henrik Clausen |
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| 245 | 1 | 0 | |a Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast |c Adnan Halim, Ida Signe Bohse Larsen, Patrick Neubert, Hiren Jitendra Joshi, Bent Larsen Petersen, Sergey Y. Vakhrushev, Sabine Strahl, and Henrik Clausen |
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| 520 | |a 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. | ||
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