The N-Glycosylation Processing Potential of the Mammalian Golgi Apparatus
Heterogeneity is an inherent feature of the glycosylation process. Mammalian cells often produce a variety of glycan structures on separate molecules of the same protein, known as glycoforms. This heterogeneity is not random but is controlled by the organization of the glycosylation machinery in the...
Main Authors: | , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Frontiers Media S.A.
2019-08-01
|
Series: | Frontiers in Cell and Developmental Biology |
Subjects: | |
Online Access: | https://www.frontiersin.org/article/10.3389/fcell.2019.00157/full |
_version_ | 1819181238349463552 |
---|---|
author | Peter Fisher Jane Thomas-Oates A. Jamie Wood A. Jamie Wood Daniel Ungar |
author_facet | Peter Fisher Jane Thomas-Oates A. Jamie Wood A. Jamie Wood Daniel Ungar |
author_sort | Peter Fisher |
collection | DOAJ |
description | Heterogeneity is an inherent feature of the glycosylation process. Mammalian cells often produce a variety of glycan structures on separate molecules of the same protein, known as glycoforms. This heterogeneity is not random but is controlled by the organization of the glycosylation machinery in the Golgi cisternae. In this work, we use a computational model of the N-glycosylation process to probe how the organization of the glycosylation machinery into different cisternae drives N-glycan biosynthesis toward differing degrees of heterogeneity. Using this model, we demonstrate the N-glycosylation potential and limits of the mammalian Golgi apparatus, for example how the number of cisternae limits the goal of achieving near homogeneity for N-glycans. The production of specific glycoforms guided by this computational study could pave the way for “glycoform engineering,” which will find uses in the functional investigation of glycans, the modulation of glycan-mediated physiological functions, and in biotechnology. |
first_indexed | 2024-12-22T22:27:03Z |
format | Article |
id | doaj.art-81c9363c60cf4645a2e750abd25e5ff7 |
institution | Directory Open Access Journal |
issn | 2296-634X |
language | English |
last_indexed | 2024-12-22T22:27:03Z |
publishDate | 2019-08-01 |
publisher | Frontiers Media S.A. |
record_format | Article |
series | Frontiers in Cell and Developmental Biology |
spelling | doaj.art-81c9363c60cf4645a2e750abd25e5ff72022-12-21T18:10:31ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2019-08-01710.3389/fcell.2019.00157462669The N-Glycosylation Processing Potential of the Mammalian Golgi ApparatusPeter Fisher0Jane Thomas-Oates1A. Jamie Wood2A. Jamie Wood3Daniel Ungar4Department of Biology, University of York, York, United KingdomDepartment of Chemistry and Centre of Excellence in Mass Spectrometry, University of York, York, United KingdomDepartment of Biology, University of York, York, United KingdomDepartment of Mathematics, University of York, York, United KingdomDepartment of Biology, University of York, York, United KingdomHeterogeneity is an inherent feature of the glycosylation process. Mammalian cells often produce a variety of glycan structures on separate molecules of the same protein, known as glycoforms. This heterogeneity is not random but is controlled by the organization of the glycosylation machinery in the Golgi cisternae. In this work, we use a computational model of the N-glycosylation process to probe how the organization of the glycosylation machinery into different cisternae drives N-glycan biosynthesis toward differing degrees of heterogeneity. Using this model, we demonstrate the N-glycosylation potential and limits of the mammalian Golgi apparatus, for example how the number of cisternae limits the goal of achieving near homogeneity for N-glycans. The production of specific glycoforms guided by this computational study could pave the way for “glycoform engineering,” which will find uses in the functional investigation of glycans, the modulation of glycan-mediated physiological functions, and in biotechnology.https://www.frontiersin.org/article/10.3389/fcell.2019.00157/fullcomputational modelingGolgi apparatusglycan biosynthesiscisternal numberglycan heterogeneity |
spellingShingle | Peter Fisher Jane Thomas-Oates A. Jamie Wood A. Jamie Wood Daniel Ungar The N-Glycosylation Processing Potential of the Mammalian Golgi Apparatus Frontiers in Cell and Developmental Biology computational modeling Golgi apparatus glycan biosynthesis cisternal number glycan heterogeneity |
title | The N-Glycosylation Processing Potential of the Mammalian Golgi Apparatus |
title_full | The N-Glycosylation Processing Potential of the Mammalian Golgi Apparatus |
title_fullStr | The N-Glycosylation Processing Potential of the Mammalian Golgi Apparatus |
title_full_unstemmed | The N-Glycosylation Processing Potential of the Mammalian Golgi Apparatus |
title_short | The N-Glycosylation Processing Potential of the Mammalian Golgi Apparatus |
title_sort | n glycosylation processing potential of the mammalian golgi apparatus |
topic | computational modeling Golgi apparatus glycan biosynthesis cisternal number glycan heterogeneity |
url | https://www.frontiersin.org/article/10.3389/fcell.2019.00157/full |
work_keys_str_mv | AT peterfisher thenglycosylationprocessingpotentialofthemammaliangolgiapparatus AT janethomasoates thenglycosylationprocessingpotentialofthemammaliangolgiapparatus AT ajamiewood thenglycosylationprocessingpotentialofthemammaliangolgiapparatus AT ajamiewood thenglycosylationprocessingpotentialofthemammaliangolgiapparatus AT danielungar thenglycosylationprocessingpotentialofthemammaliangolgiapparatus AT peterfisher nglycosylationprocessingpotentialofthemammaliangolgiapparatus AT janethomasoates nglycosylationprocessingpotentialofthemammaliangolgiapparatus AT ajamiewood nglycosylationprocessingpotentialofthemammaliangolgiapparatus AT ajamiewood nglycosylationprocessingpotentialofthemammaliangolgiapparatus AT danielungar nglycosylationprocessingpotentialofthemammaliangolgiapparatus |