Cited by 67Glycosylation and Glycoproteins ResearchViral Infectious Diseases and Gene Expression in InsectsCellular transport and secretion

Analysis of site-specific N-glycan remodeling in the endoplasmic reticulum and the Golgi

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Hang, Ivan, Lin, Chia-wei, Grant, Oliver C, Fleurkens, Susanna, Villiger, Thomas K, Soos, Miroslav, Morbidelli, Massimo, Woods, Robert J +2 more·2015·Glycobiology

Abstract

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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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
Published
2015-08-03
Volume
25
Issue
12
Pages
1335-1349
ISSN
  • 0959-6658 (ISSN-L)
  • 1460-2423
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
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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