Interplay between de novo and salvage pathways of GDP-fucose synthesis.


Journal

PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081

Informations de publication

Date de publication:
2024
Historique:
received: 05 06 2024
accepted: 12 08 2024
medline: 25 10 2024
pubmed: 25 10 2024
entrez: 24 10 2024
Statut: epublish

Résumé

GDP-fucose is synthesised via two pathways: de novo and salvage. The first uses GDP-mannose as a substrate, and the second uses free fucose. To date, these pathways have been considered to work separately and not to have an influence on each other. We report the mutual response of the de novo and salvage pathways to the lack of enzymes from a particular route of GDP-fucose synthesis. We detected different efficiencies of GDP-fucose and fucosylated structure synthesis after a single inactivation of enzymes of the de novo pathway. Our study demonstrated the unequal influence of the salvage enzymes on the production of GDP-fucose by enzymes of the de novo biosynthesis pathway. Simultaneously, we detected an elevated level of one of the enzymes of the de novo pathway in the cell line lacking the enzyme of the salvage biosynthesis pathway. Additionally, we identified dissimilarities in fucose uptake between cells lacking TSTA3 and GMDS proteins.

Identifiants

pubmed: 39446915
doi: 10.1371/journal.pone.0309450
pii: PONE-D-24-22138
doi:

Substances chimiques

Guanosine Diphosphate Fucose 15839-70-0
Fucose 28RYY2IV3F
Fucosyltransferases EC 2.4.1.-
GDPmannose 4,6-dehydratase EC 4.2.1.47
Guanosine Diphosphate Mannose 3123-67-9
Hydro-Lyases EC 4.2.1.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

e0309450

Informations de copyright

Copyright: © 2024 Skurska, Olczak. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Déclaration de conflit d'intérêts

The authors have declared that no competing interests exist.

Auteurs

Edyta Skurska (E)

Department of Biochemistry, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.

Mariusz Olczak (M)

Department of Biochemistry, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.

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Classifications MeSH