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Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae

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-...

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Autores principales: Neubert, Patrick, Halim, Adnan, Zauser, Martin, Essig, Andreas, Joshi, Hiren J., Zatorska, Ewa, Larsen, Ida Signe Bohse, Loibl, Martin, Castells-Ballester, Joan, Aebi, Markus, Clausen, Henrik, Strahl, Sabine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Biochemistry and Molecular Biology 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4824858/
https://www.ncbi.nlm.nih.gov/pubmed/26764011
http://dx.doi.org/10.1074/mcp.M115.057505
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author Neubert, Patrick
Halim, Adnan
Zauser, Martin
Essig, Andreas
Joshi, Hiren J.
Zatorska, Ewa
Larsen, Ida Signe Bohse
Loibl, Martin
Castells-Ballester, Joan
Aebi, Markus
Clausen, Henrik
Strahl, Sabine
author_facet Neubert, Patrick
Halim, Adnan
Zauser, Martin
Essig, Andreas
Joshi, Hiren J.
Zatorska, Ewa
Larsen, Ida Signe Bohse
Loibl, Martin
Castells-Ballester, Joan
Aebi, Markus
Clausen, Henrik
Strahl, Sabine
author_sort Neubert, Patrick
collection PubMed
description 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.
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spelling pubmed-48248582016-04-21 Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae Neubert, Patrick Halim, Adnan Zauser, Martin Essig, Andreas Joshi, Hiren J. Zatorska, Ewa Larsen, Ida Signe Bohse Loibl, Martin Castells-Ballester, Joan Aebi, Markus Clausen, Henrik Strahl, Sabine Mol Cell Proteomics Research 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. The American Society for Biochemistry and Molecular Biology 2016-04 2016-01-13 /pmc/articles/PMC4824858/ /pubmed/26764011 http://dx.doi.org/10.1074/mcp.M115.057505 Text en © 2016 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version free via Creative Commons CC-BY license (http://creativecommons.org/licenses/by/4.0) .
spellingShingle Research
Neubert, Patrick
Halim, Adnan
Zauser, Martin
Essig, Andreas
Joshi, Hiren J.
Zatorska, Ewa
Larsen, Ida Signe Bohse
Loibl, Martin
Castells-Ballester, Joan
Aebi, Markus
Clausen, Henrik
Strahl, Sabine
Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae
title Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae
title_full Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae
title_fullStr Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae
title_full_unstemmed Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae
title_short Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae
title_sort mapping the o-mannose glycoproteome in saccharomyces cerevisiae
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4824858/
https://www.ncbi.nlm.nih.gov/pubmed/26764011
http://dx.doi.org/10.1074/mcp.M115.057505
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