Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae

Research output: Contribution to journalJournal articlepeer-review

Standard

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.

In: Molecular and Cellular Proteomics, Vol. 15, No. 4, 04.2016, p. 1323-37.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Neubert, P, Halim, A, Zauser, M, Essig, A, Joshi, HJ, Zatorska, E, Larsen, ISB, Loibl, M, Castells-Ballester, J, Aebi, M, Clausen, H & Strahl, S 2016, 'Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae', Molecular and Cellular Proteomics, vol. 15, no. 4, pp. 1323-37. https://doi.org/10.1074/mcp.M115.057505

APA

Neubert, P., Halim, A., Zauser, M., Essig, A., Joshi, H. J., Zatorska, E., Larsen, I. S. B., Loibl, M., Castells-Ballester, J., Aebi, M., Clausen, H., & Strahl, S. (2016). Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae. Molecular and Cellular Proteomics, 15(4), 1323-37. https://doi.org/10.1074/mcp.M115.057505

Vancouver

Neubert P, Halim A, Zauser M, Essig A, Joshi HJ, Zatorska E et al. Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae. Molecular and Cellular Proteomics. 2016 Apr;15(4):1323-37. https://doi.org/10.1074/mcp.M115.057505

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. / Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae. In: Molecular and Cellular Proteomics. 2016 ; Vol. 15, No. 4. pp. 1323-37.

Bibtex

@article{fec881bf3d9c44f1852ba245d7a6ef85,
title = "Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae",
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 mammalsO-mannosylation is the only type ofO-glycosylation. In an essential step toward the full understanding of proteinO-mannosylation we mapped theO-mannose glycoproteome in baker's yeast. Taking advantage of anO-glycan elongation deficient yeast strain to simplify sample complexity, we identified over 500O-glycoproteins from all subcellular compartments for which over 2300O-mannosylation sites were mapped by electron-transfer dissociation (ETD)-based MS/MS. In this study, we focus on the 293O-glycoproteins (over 1900 glycosylation sites identified by ETD-MS/MS) that enter the secretory pathway and are targets of ER-localized proteinO-mannosyltransferases. We find thatO-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 thatO-mannosylation is favored in unstructured regions and β-strands. Furthermore,O-mannosylation is impeded in the proximity ofN-glycosylation sites suggesting the interplay of these types of post-translational modifications. The detailed knowledge of the target proteins and theirO-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 ofO-glycosylation from yeast to mammals.",
author = "Patrick Neubert and Adnan Halim and Martin Zauser and Andreas Essig and Joshi, {Hiren J} and Ewa Zatorska and Larsen, {Ida Signe Bohse} and Martin Loibl and Joan Castells-Ballester and Markus Aebi and Henrik Clausen and Sabine Strahl",
note = "{\textcopyright} 2016 by The American Society for Biochemistry and Molecular Biology, Inc.",
year = "2016",
month = apr,
doi = "10.1074/mcp.M115.057505",
language = "English",
volume = "15",
pages = "1323--37",
journal = "Molecular and Cellular Proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology",
number = "4",

}

RIS

TY - JOUR

T1 - Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae

AU - Neubert, Patrick

AU - Halim, Adnan

AU - Zauser, Martin

AU - Essig, Andreas

AU - Joshi, Hiren J

AU - Zatorska, Ewa

AU - Larsen, Ida Signe Bohse

AU - Loibl, Martin

AU - Castells-Ballester, Joan

AU - Aebi, Markus

AU - Clausen, Henrik

AU - Strahl, Sabine

N1 - © 2016 by The American Society for Biochemistry and Molecular Biology, Inc.

PY - 2016/4

Y1 - 2016/4

N2 - 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 mammalsO-mannosylation is the only type ofO-glycosylation. In an essential step toward the full understanding of proteinO-mannosylation we mapped theO-mannose glycoproteome in baker's yeast. Taking advantage of anO-glycan elongation deficient yeast strain to simplify sample complexity, we identified over 500O-glycoproteins from all subcellular compartments for which over 2300O-mannosylation sites were mapped by electron-transfer dissociation (ETD)-based MS/MS. In this study, we focus on the 293O-glycoproteins (over 1900 glycosylation sites identified by ETD-MS/MS) that enter the secretory pathway and are targets of ER-localized proteinO-mannosyltransferases. We find thatO-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 thatO-mannosylation is favored in unstructured regions and β-strands. Furthermore,O-mannosylation is impeded in the proximity ofN-glycosylation sites suggesting the interplay of these types of post-translational modifications. The detailed knowledge of the target proteins and theirO-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 ofO-glycosylation from yeast to mammals.

AB - 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 mammalsO-mannosylation is the only type ofO-glycosylation. In an essential step toward the full understanding of proteinO-mannosylation we mapped theO-mannose glycoproteome in baker's yeast. Taking advantage of anO-glycan elongation deficient yeast strain to simplify sample complexity, we identified over 500O-glycoproteins from all subcellular compartments for which over 2300O-mannosylation sites were mapped by electron-transfer dissociation (ETD)-based MS/MS. In this study, we focus on the 293O-glycoproteins (over 1900 glycosylation sites identified by ETD-MS/MS) that enter the secretory pathway and are targets of ER-localized proteinO-mannosyltransferases. We find thatO-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 thatO-mannosylation is favored in unstructured regions and β-strands. Furthermore,O-mannosylation is impeded in the proximity ofN-glycosylation sites suggesting the interplay of these types of post-translational modifications. The detailed knowledge of the target proteins and theirO-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 ofO-glycosylation from yeast to mammals.

U2 - 10.1074/mcp.M115.057505

DO - 10.1074/mcp.M115.057505

M3 - Journal article

C2 - 26764011

VL - 15

SP - 1323

EP - 1337

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

SN - 1535-9476

IS - 4

ER -

ID: 160105895