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Glycobiology. 2015 Dec;25(12):1335-49. doi: 10.1093/glycob/cwv058. Epub 2015 Aug 3.

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

Author information

1
Institute of Microbiology, Department of Biology.
2
Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, USA.
3
Institute for Chemical and Bioengineering, Department of Chemistry and Applied Biosciences, Swiss Federal Institute of Technology, ETH Zurich, CH-8093 Zurich, Switzerland.
4
Institute of Microbiology, Department of Biology markus.aebi@micro.biol.ethz.ch robert.gauss@micro.biol.ethz.ch.

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.

KEYWORDS:

Golgi; Golgi glycosylation; endoplasmic reticulum glycosylation; site-specific glycosylation

PMID:
26240167
PMCID:
PMC4634314
DOI:
10.1093/glycob/cwv058
[Indexed for MEDLINE]
Free PMC Article

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