| Online-Ressource |
Verfasst von: | Neubert, Patrick [VerfasserIn]  |
| Zatorska, Ewa [VerfasserIn]  |
| Loibl, Martin [VerfasserIn]  |
| Castells Ballester, Joan [VerfasserIn]  |
| 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 |
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. |
DOI: | doi:10.1074/mcp.M115.057505 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Kostenfrei: Verlag: http://dx.doi.org/10.1074/mcp.M115.057505 |
| Kostenfrei: Verlag: http://www.mcponline.org/content/15/4/1323 |
| DOI: https://doi.org/10.1074/mcp.M115.057505 |
Datenträger: | Online-Ressource |
Sprache: | eng |
K10plus-PPN: | 1559873396 |
Verknüpfungen: | → Zeitschrift |
Mapping the O-Mannose glycoproteome in saccharomyces cerevisiae / Neubert, Patrick [VerfasserIn] (Online-Ressource)