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Origin of cytoplasmic GDP-fucose determines its contribution to glycosylation reactions
Biosynthesis of macromolecules requires precursors such as sugars or amino acids, originating from exogenous/dietary sources, reutilization/salvage of degraded molecules, or de novo synthesis. Since these sources are assumed to contribute to one homogenous pool, their individual contributions are of...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9441714/ https://www.ncbi.nlm.nih.gov/pubmed/36053214 http://dx.doi.org/10.1083/jcb.202205038 |
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author | Sosicka, Paulina Ng, Bobby G. Pepi, Lauren E. Shajahan, Asif Wong, Maurice Scott, David A. Matsumoto, Kenjiroo Xia, Zhi-Jie Lebrilla, Carlito B. Haltiwanger, Robert S. Azadi, Parastoo Freeze, Hudson H. |
author_facet | Sosicka, Paulina Ng, Bobby G. Pepi, Lauren E. Shajahan, Asif Wong, Maurice Scott, David A. Matsumoto, Kenjiroo Xia, Zhi-Jie Lebrilla, Carlito B. Haltiwanger, Robert S. Azadi, Parastoo Freeze, Hudson H. |
author_sort | Sosicka, Paulina |
collection | PubMed |
description | Biosynthesis of macromolecules requires precursors such as sugars or amino acids, originating from exogenous/dietary sources, reutilization/salvage of degraded molecules, or de novo synthesis. Since these sources are assumed to contribute to one homogenous pool, their individual contributions are often overlooked. Protein glycosylation uses monosaccharides from all the above sources to produce nucleotide sugars required to assemble hundreds of distinct glycans. Here, we demonstrate that cells identify the origin/heritage of the monosaccharide, fucose, for glycosylation. We measured the contribution of GDP-fucose from each of these sources for glycan synthesis and found that different fucosyltransferases, individual glycoproteins, and linkage-specific fucose residues identify and select different GDP-fucose pools dependent on their heritage. This supports the hypothesis that GDP-fucose exists in multiple, distinct pools, not as a single homogenous pool. The selection is tightly regulated since the overall pool size remains constant. We present novel perspectives on monosaccharide metabolism, which may have a general applicability. |
format | Online Article Text |
id | pubmed-9441714 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-94417142023-03-02 Origin of cytoplasmic GDP-fucose determines its contribution to glycosylation reactions Sosicka, Paulina Ng, Bobby G. Pepi, Lauren E. Shajahan, Asif Wong, Maurice Scott, David A. Matsumoto, Kenjiroo Xia, Zhi-Jie Lebrilla, Carlito B. Haltiwanger, Robert S. Azadi, Parastoo Freeze, Hudson H. J Cell Biol Article Biosynthesis of macromolecules requires precursors such as sugars or amino acids, originating from exogenous/dietary sources, reutilization/salvage of degraded molecules, or de novo synthesis. Since these sources are assumed to contribute to one homogenous pool, their individual contributions are often overlooked. Protein glycosylation uses monosaccharides from all the above sources to produce nucleotide sugars required to assemble hundreds of distinct glycans. Here, we demonstrate that cells identify the origin/heritage of the monosaccharide, fucose, for glycosylation. We measured the contribution of GDP-fucose from each of these sources for glycan synthesis and found that different fucosyltransferases, individual glycoproteins, and linkage-specific fucose residues identify and select different GDP-fucose pools dependent on their heritage. This supports the hypothesis that GDP-fucose exists in multiple, distinct pools, not as a single homogenous pool. The selection is tightly regulated since the overall pool size remains constant. We present novel perspectives on monosaccharide metabolism, which may have a general applicability. Rockefeller University Press 2022-09-02 /pmc/articles/PMC9441714/ /pubmed/36053214 http://dx.doi.org/10.1083/jcb.202205038 Text en © 2022 Sosicka et al. https://creativecommons.org/licenses/by-nc-sa/4.0/http://www.rupress.org/terms/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Sosicka, Paulina Ng, Bobby G. Pepi, Lauren E. Shajahan, Asif Wong, Maurice Scott, David A. Matsumoto, Kenjiroo Xia, Zhi-Jie Lebrilla, Carlito B. Haltiwanger, Robert S. Azadi, Parastoo Freeze, Hudson H. Origin of cytoplasmic GDP-fucose determines its contribution to glycosylation reactions |
title | Origin of cytoplasmic GDP-fucose determines its contribution to glycosylation reactions |
title_full | Origin of cytoplasmic GDP-fucose determines its contribution to glycosylation reactions |
title_fullStr | Origin of cytoplasmic GDP-fucose determines its contribution to glycosylation reactions |
title_full_unstemmed | Origin of cytoplasmic GDP-fucose determines its contribution to glycosylation reactions |
title_short | Origin of cytoplasmic GDP-fucose determines its contribution to glycosylation reactions |
title_sort | origin of cytoplasmic gdp-fucose determines its contribution to glycosylation reactions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9441714/ https://www.ncbi.nlm.nih.gov/pubmed/36053214 http://dx.doi.org/10.1083/jcb.202205038 |
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