Mapping the O-Mannose glycoproteome in saccharomyces cerevisiae

• Verfasst von: Neubert, Patrick [VerfasserIn]
• Verfasst von: Zatorska, Ewa [VerfasserIn]
• Verfasst von: Loibl, Martin [VerfasserIn]
• Verfasst von: Castells Ballester, Joan [VerfasserIn]
• Verfasst von: Strahl, Sabine [VerfasserIn]
• Titel: Mapping the O-Mannose glycoproteome in saccharomyces cerevisiae
• Verf.angabe: Patrick Neubert, Adnan Halim, Martin Zauser, Andreas Essig, Hiren J. Joshi, Ewa Zatorska, Ida Signe Bohse Larsen, Martin Loibl, Joan Castells-Ballester, Markus Aebi, Henrik Clausen, and Sabine Strahl
• Umfang: 15 S.
• Fussnoten: Gesehen am 19.06.2017
• Titel Quelle: Enthalten in: Molecular & cellular proteomics
• Jahr Quelle: 2016
• Band/Heft Quelle: 15(2016), 4, S. 1323-1337
• ISSN Quelle: 1535-9484
• DOI: doi:10.1074/mcp.M115.057505
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1559873396

Abstract

O-Mannosylation is a vital protein modification conserved from fungi to humans. Yeast is a perfect model to study this post-translational modification, because in contrast to mammals O-mannosylation is the only type of O-glycosylation. In an essential step toward the full understanding of protein O-mannosylation we mapped the O-mannose glycoproteome in baker's yeast. Taking advantage of an O-glycan elongation deficient yeast strain to simplify sample complexity, we identified over 500 O-glycoproteins from all subcellular compartments for which over 2300 O-mannosylation sites were mapped by electron-transfer dissociation (ETD)-based MS/MS. In this study, we focus on the 293 O-glycoproteins (over 1900 glycosylation sites identified by ETD-MS/MS) that enter the secretory pathway and are targets of ER-localized protein O-mannosyltransferases. We find that O-mannosylation is not only a prominent modification of cell wall and plasma membrane proteins, but also of a large number of proteins from the secretory pathway with crucial functions in protein glycosylation, folding, quality control, and trafficking. The analysis of glycosylation sites revealed that O-mannosylation is favored in unstructured regions and β-strands. Furthermore, O-mannosylation is impeded in the proximity of N-glycosylation sites suggesting the interplay of these types of post-translational modifications. The detailed knowledge of the target proteins and their O-mannosylation sites opens for discovery of new roles of this essential modification in eukaryotes, and for a first glance on the evolution of different types of O-glycosylation from yeast to mammals.