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...

Full description

Bibliographic Details
Main Authors: Peter Fisher, Jane Thomas-Oates, A. Jamie Wood, Daniel Ungar
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