Navigation überspringen
Universitätsbibliothek Heidelberg
Status: Bibliographieeintrag

Verfügbarkeit
Standort: ---
Exemplare: ---
heiBIB
 Online-Ressource
Verfasst von:Neubert, Patrick [VerfasserIn]   i
 Zatorska, Ewa [VerfasserIn]   i
 Loibl, Martin [VerfasserIn]   i
 Castells Ballester, Joan [VerfasserIn]   i
 Strahl, Sabine [VerfasserIn]   i
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

Permanenter Link auf diesen Titel (bookmarkfähig):  https://katalog.ub.uni-heidelberg.de/titel/68129240   QR-Code
zum Seitenanfang