Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology. / Steentoft, Catharina; Vakhrushev, Sergey Y; Joshi, Hiren J; Kong, Yun; Vester-Christensen, Malene B; Schjoldager, Katrine Ter-Borch Gram; Lavrsen, Kirstine; Dabelsteen, Sally; Pedersen, Nis Borbye; da Silva, Lara Patricia Marcos; Gupta, Ramneek; Paul Bennett, Eric; Mandel, Ulla; Brunak, Søren; Wandall, Hans H; Levery, Steven B; Clausen, Henrik.

In: E M B O Journal, Vol. 32, No. 10, 15.05.2013, p. 1478-1488.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Steentoft, C, Vakhrushev, SY, Joshi, HJ, Kong, Y, Vester-Christensen, MB, Schjoldager, KT-BG, Lavrsen, K, Dabelsteen, S, Pedersen, NB, da Silva, LPM, Gupta, R, Paul Bennett, E, Mandel, U, Brunak, S, Wandall, HH, Levery, SB & Clausen, H 2013, 'Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology', E M B O Journal, vol. 32, no. 10, pp. 1478-1488. https://doi.org/10.1038/emboj.2013.79

APA

Steentoft, C., Vakhrushev, S. Y., Joshi, H. J., Kong, Y., Vester-Christensen, M. B., Schjoldager, K. T-B. G., Lavrsen, K., Dabelsteen, S., Pedersen, N. B., da Silva, L. P. M., Gupta, R., Paul Bennett, E., Mandel, U., Brunak, S., Wandall, H. H., Levery, S. B., & Clausen, H. (2013). Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology. E M B O Journal, 32(10), 1478-1488. https://doi.org/10.1038/emboj.2013.79

Vancouver

Steentoft C, Vakhrushev SY, Joshi HJ, Kong Y, Vester-Christensen MB, Schjoldager KT-BG et al. Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology. E M B O Journal. 2013 May 15;32(10):1478-1488. https://doi.org/10.1038/emboj.2013.79

Author

Steentoft, Catharina ; Vakhrushev, Sergey Y ; Joshi, Hiren J ; Kong, Yun ; Vester-Christensen, Malene B ; Schjoldager, Katrine Ter-Borch Gram ; Lavrsen, Kirstine ; Dabelsteen, Sally ; Pedersen, Nis Borbye ; da Silva, Lara Patricia Marcos ; Gupta, Ramneek ; Paul Bennett, Eric ; Mandel, Ulla ; Brunak, Søren ; Wandall, Hans H ; Levery, Steven B ; Clausen, Henrik. / Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology. In: E M B O Journal. 2013 ; Vol. 32, No. 10. pp. 1478-1488.

Bibtex

@article{e57a7f70ca934562a6e13dfbaca85f84,
title = "Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology",
abstract = "Glycosylation is the most abundant and diverse posttranslational modification of proteins. While several types of glycosylation can be predicted by the protein sequence context, and substantial knowledge of these glycoproteomes is available, our knowledge of the GalNAc-type O-glycosylation is highly limited. This type of glycosylation is unique in being regulated by 20 polypeptide GalNAc-transferases attaching the initiating GalNAc monosaccharides to Ser and Thr (and likely some Tyr) residues. We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis. We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation. The finding of unique subsets of O-glycoproteins in each cell line provides evidence that the O-glycoproteome is differentially regulated and dynamic. The greatly expanded view of the O-glycoproteome should facilitate the exploration of how site-specific O-glycosylation regulates protein function.",
author = "Catharina Steentoft and Vakhrushev, {Sergey Y} and Joshi, {Hiren J} and Yun Kong and Vester-Christensen, {Malene B} and Schjoldager, {Katrine Ter-Borch Gram} and Kirstine Lavrsen and Sally Dabelsteen and Pedersen, {Nis Borbye} and {da Silva}, {Lara Patricia Marcos} and Ramneek Gupta and {Paul Bennett}, Eric and Ulla Mandel and S{\o}ren Brunak and Wandall, {Hans H} and Levery, {Steven B} and Henrik Clausen",
year = "2013",
month = may,
day = "15",
doi = "10.1038/emboj.2013.79",
language = "English",
volume = "32",
pages = "1478--1488",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "10",

}

RIS

TY - JOUR

T1 - Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology

AU - Steentoft, Catharina

AU - Vakhrushev, Sergey Y

AU - Joshi, Hiren J

AU - Kong, Yun

AU - Vester-Christensen, Malene B

AU - Schjoldager, Katrine Ter-Borch Gram

AU - Lavrsen, Kirstine

AU - Dabelsteen, Sally

AU - Pedersen, Nis Borbye

AU - da Silva, Lara Patricia Marcos

AU - Gupta, Ramneek

AU - Paul Bennett, Eric

AU - Mandel, Ulla

AU - Brunak, Søren

AU - Wandall, Hans H

AU - Levery, Steven B

AU - Clausen, Henrik

PY - 2013/5/15

Y1 - 2013/5/15

N2 - Glycosylation is the most abundant and diverse posttranslational modification of proteins. While several types of glycosylation can be predicted by the protein sequence context, and substantial knowledge of these glycoproteomes is available, our knowledge of the GalNAc-type O-glycosylation is highly limited. This type of glycosylation is unique in being regulated by 20 polypeptide GalNAc-transferases attaching the initiating GalNAc monosaccharides to Ser and Thr (and likely some Tyr) residues. We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis. We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation. The finding of unique subsets of O-glycoproteins in each cell line provides evidence that the O-glycoproteome is differentially regulated and dynamic. The greatly expanded view of the O-glycoproteome should facilitate the exploration of how site-specific O-glycosylation regulates protein function.

AB - Glycosylation is the most abundant and diverse posttranslational modification of proteins. While several types of glycosylation can be predicted by the protein sequence context, and substantial knowledge of these glycoproteomes is available, our knowledge of the GalNAc-type O-glycosylation is highly limited. This type of glycosylation is unique in being regulated by 20 polypeptide GalNAc-transferases attaching the initiating GalNAc monosaccharides to Ser and Thr (and likely some Tyr) residues. We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis. We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation. The finding of unique subsets of O-glycoproteins in each cell line provides evidence that the O-glycoproteome is differentially regulated and dynamic. The greatly expanded view of the O-glycoproteome should facilitate the exploration of how site-specific O-glycosylation regulates protein function.

U2 - 10.1038/emboj.2013.79

DO - 10.1038/emboj.2013.79

M3 - Journal article

C2 - 23584533

VL - 32

SP - 1478

EP - 1488

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 10

ER -

ID: 45521373