Unmasking Fucosylation: from Cell Adhesion to Immune System Regulation and Diseases
Open accessAbstract
Fucosylation is a biological process broadly observed in vertebrates, invertebrates, plants, bacteria, and fungi. Fucose moieties on cell-surface glycans are increasingly recognized as critical to many cell-cell interaction and signaling processes. One of the characteristic roles of fucose is its regulation of selectin-dependent leukocyte adhesion that has been well studied over the last two decades. Recent studies of fucose in immune cell development and function regulation have significantly expanded the contemporary understanding of fucosylation. From cellular adhesion to immune regulation, herein we discuss the use of gene knockout studies, competitive inhibitors of fucose-containing glycan, and metabolic inhibitors of fucose biosynthesis to probe fucosylated glycan biosynthesis and signaling and its functional consequences. Promising clinical and preclinical applications in sickle cell disease, rheumatoid arthritis, tumor inhibition, metastasis prevention, antibody-dependent cell-mediated cytotoxicity, chemoresistance reversal, and in improving chemotherapy-related side effects and recovery are reviewed.
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GMDS encodes GDP-mannose 4,6-dehydratase, which catalyzes the first step in the GDP-fucose de novo synthesis pathway.
“GMDS encodes GDP-mannose 4,6-dehydratase, which catalyzes the first step in the GDP-fucose de novo synthesis pathway53 (Fig. S7B).”
From Large-scale CRISPR screening in primary human 3D gastric organoids enables comprehensive dissection of gene-drug interactions (2025) · cites this paper as [53]
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Lo, Y.-H., Horn, H. T., Huang, M.-F., Yu, W.-C., Young, C.-M., Liu, Q., Tomaske, M., Towers, M., Dominguez, A., Bassik, M. C., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62818-3 · Cited by 37 · see citing works
“GMDS encodes GDP-mannose 4,6-dehydratase, which catalyzes the fi rst step in the GDP-fucose de novo synthesis pathway 53 (Fig.”
- Authors
- Li, J., Hsu, H.-C., Mountz, J. D., & Allen, J. G.
- Affiliations
- University of Alabama at Birmingham (US)
- Amgen (United States) (US)
- Corresponding author
- Allen, John G.
- Venue
- Cell Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2018-05
- Volume
- 25
- Issue
- 5
- Pages
- 499-512
- ISSN
- 2451-9448 (ISSN-L)
- 2451-9456
- OpenAlex
- W2794128825
- Cited by
- 256
- References
- 5
- Citations by year
- 2026: 25 · 2025: 39 · 2024: 43 · 2023: 36 · 2022: 48 · 2021: 23 · 2020: 26 · 2019: 15 · 2018: 1
- FWCI
- 1.59
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell chemical biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- fucosylation, fucose, cell surface glycans, cell adhesion, immune regulation, immune cell development, fucose biosynthesis, sickle cell disease, rheumatoid arthritis, tumor growth inhibition, metastasis prevention, antibody-dependent cellular cytotoxicity, chemoresistance, chemotherapy side effects
- MeSH terms
- Anemia, Sickle Cell, Animals, Arthritis, Rheumatoid, Cell Adhesion, Fucose, Glycosylation, Humans, Immunity, Cellular, Immunity, Innate, Macrophages, Neoplasms, Polysaccharides, Selectins
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