Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast

• Verfasst von: Halim, Adnan [VerfasserIn]
• Verfasst von: Neubert, Patrick [VerfasserIn]
• Verfasst von: Strahl, Sabine [VerfasserIn]
• Titel: Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast
• Verf.angabe: Adnan Halim, Ida Signe Bohse Larsen, Patrick Neubert, Hiren Jitendra Joshi, Bent Larsen Petersen, Sergey Y. Vakhrushev, Sabine Strahl, and Henrik Clausen
• Umfang: 6 S.
• Fussnoten: Gesehen am TT.MM.JJJ
• Titel Quelle: Enthalten in: National Academy of Sciences (Washington, DC): Proceedings of the National Academy of Sciences of the United States of America
• Jahr Quelle: 2015
• Band/Heft Quelle: 112(2015), 51, S. 15648-15653
• ISSN Quelle: 1091-6490
• DOI: doi:10.1073/pnas.1511743112
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1559796480

Abstract

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.