Analysis of site-specific N-glycan remodeling in the endoplasmic reticulum and the Golgi
Open accessAbstract
The hallmark of N-linked protein glycosylation is the generation of diverse glycan structures in the secretory pathway. Dynamic, non-template-driven processes of N-glycan remodeling in the endoplasmic reticulum and the Golgi provide the cellular setting for structural diversity. We applied newly developed mass spectrometry-based analytics to quantify site-specific N-glycan remodeling of the model protein Pdi1p expressed in insect cells. Molecular dynamics simulation, mutational analysis, kinetic studies of in vitro processing events and glycan flux analysis supported the defining role of the protein in N-glycan processing.
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Glycosylation sites can vary in accessibility and the surrounding amino acid environment on the surface of a protein.
“Glycosylation sites can vary both in accessibility and the surrounding amino acid environment on the surface of a protein [109].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [109]
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North, S. J., Huang, H.-H., Sundaram, S., Jang-Lee, J., Etienne, A. T., Trollope, A., Chalabi, S., Dell, A., Stanley, P., & Haslam, S. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.068353 · Cited by 207 · see citing works
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Visualization of the HIV-1 Env glycan shield across scales
Berndsen, Z. T., Chakraborty, S., Wang, X., Cottrell, C. A., Torres, J. L., Diedrich, J. K., López, C. A., Yates, J. R., van Gils, M. J., Paulson, J. C., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2000260117 · Cited by 86 · see citing works
Glycoengineering Chinese hamster ovary cells: a short history
Donini, R., Haslam, S. M., & Kontoravdi, C. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200840 · Cited by 37 · see citing works
- Authors
- Hang, I., Lin, C.-W., Grant, O. C., Fleurkens, S., Villiger, T. K., Soos, M., Morbidelli, M., Woods, R. J., Gauss, R., & Aebi, M.
- Affiliations
- Institute of Microbiology (CN)
- University of Georgia (US)
- ETH Zurich (CH)
- Corresponding author
- Gauss, Robert
- Aebi, Markus
- Venue
- Glycobiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2015-08-03
- Volume
- 25
- Issue
- 12
- Pages
- 1335-1349
- ISSN
- 0959-6658 (ISSN-L)
- 1460-2423
- PMC
- PMC4634314
- OpenAlex
- W2218010822
- Cited by
- 67
- References
- 1
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 6 · 2023: 4 · 2022: 3 · 2021: 10 · 2020: 10 · 2019: 5 · 2018: 5 · 2017: 5 · 2016: 12 · 2015: 1
- FWCI
- 3.33
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Glycobiology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- reroDoc Digital Library (submittedVersion)
- Repository for Publications and Research Data (ETH Zurich) (submittedVersion, other-oa)
- ETH Zürich Research Collection
- Funders
- National Institutes of Health (P41GM103390, R01GM094919)
- Science Foundation of Ireland (08/IN.1/B2070)
- ETH Research (07 10-1)
- Swiss National Science Foundation (31003A_127098)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- N-glycosylation, endoplasmic reticulum, Golgi apparatus, glycan processing, secretory pathway, insect cell expression, molecular dynamics simulation, mutation analysis
- MeSH terms
- Animals, Endoplasmic Reticulum, Glycosylation, Golgi Apparatus, Polysaccharides, Protein Processing, Post-Translational, Spodoptera, Protein Disulfide-Isomerases, Saccharomyces cerevisiae Proteins, Sf9 Cells
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