ArticleThe Journal of biological chemistry2020
Characterizing human α-1,6-fucosyltransferase (FUT8) substrate specificity and structural similarities with related fucosyltransferases.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 46 citations in OpenAlex.
- One-Step Microfluidic Manufactured Fucose-Decorated Sweetosomes Choose the Time and the Road for Their Intracellular Journey to Cancer Treatment.Advanced healthcare materials · 2026Article
- Signal peptide peptidase- and SPP-like 3-dependent shedding of α1,6-fucosyltransferase differentially affects core fucosylation.The Journal of biological chemistry · 2026Article
- FUT8 Catalysis Involves GDP-Fucose-Induced Loop Activation Promoting a Reaction at the SACS catalysis · 2026Article
- Exploiting human fucosyltransferase 8 allostery with a covalent inhibitor for core fucosylation suppression.Nature communications · 2026Article
- Structure, function, and implications of fucosyltransferases in health and disease.Nature communications · 2025Review
- Chemoenzymatic Synthesis of Asymmetric Bisecting Bi-, Tri-, and Tetra-AntennaryJournal of the American Chemical Society · 2025Article
- Review
- FUT10 and FUT11 are protein O-fucosyltransferases that modify protein EMI domains.Nature chemical biology · 2025Article
- Requirement for Fucosyltransferase 2 in Allergic Airway Hyperreactivity and Mucus Obstruction.American journal of respiratory cell and molecular biology · 2025Article
- ProteinMolecules (Basel, Switzerland) · 2025Review
- BisectingACS chemical biology · 2025Article
- Crystal structure of the fungal mannosyltransferase Och1 reveals active site primed for N-glycan binding.PloS one · 2025Article
- Candidate genes involved in biosynthesis and degradation of the main extracellular matrix polysaccharides of brown algae and their probable evolutionary history.BMC genomics · 2024Article
- Regulation of intracellular activity of N-glycan branching enzymes in mammals.The Journal of biological chemistry · 2024Review
- Glycosyltransferase 8 domain-containing protein 1 (GLT8D1) is a UDP-dependent galactosyltransferase.Scientific reports · 2023Article
- Modulating antibody effector functions by Fc glycoengineering.Biotechnology advances · 2023Review
- Structural basis for Lewis antigen synthesis by the α1,3-fucosyltransferase FUT9.Nature chemical biology · 2023Article
- Core Fucosylation Mediated by the FucT-8 Enzyme Affects TRAIL-Induced Apoptosis and Sensitivity to Chemotherapy in Human SW480 and SW620 Colorectal Cancer Cells.International journal of molecular sciences · 2023Article
- Beyond antibody fucosylation: α-(1,6)-fucosyltransferase (Fut8) as a potential new therapeutic target for cancer immunotherapy.Antibody therapeutics · 2023Review
- The BNT162b2 mRNA SARS-CoV-2 vaccine induces transient afucosylated IgG1 in naive but not in antigen-experienced vaccinees.EBioMedicine · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
Mammalian Asn-linked glycans are extensively processed as they transit the secretory pathway to generate diverse glycans on cell surface and secreted glycoproteins. Additional modification of the glycan core by α-1,6-fucose addition to the innermost GlcNAc residue (core fucosylation) is catalyzed by an α-1,6-fucosyltransferase (FUT8). The importance of core fucosylation can be seen in the complex pathological phenotypes of FUT8 null mice, which display defects in cellular signaling, development, and subsequent neonatal lethality. Elevated core fucosylation has also been identified in several human cancers. However, the structural basis for FUT8 substrate specificity remains unknown.Here, using various crystal structures of FUT8 in complex with a donor substrate analog, and with four distinct glycan acceptors, we identify the molecular basis for FUT8 specificity and activity. The ordering of three active site loops corresponds to an increased occupancy for bound GDP, suggesting an induced-fit folding of the donor-binding subsite. Structures of the various acceptor complexes were compared with kinetic data on FUT8 active site mutants and with specificity data from a library of glycan acceptors to reveal how binding site complementarity and steric hindrance can tune substrate affinity. The FUT8 structure was also compared with other known fucosyltransferases to identify conserved and divergent structural features for donor and acceptor recognition and catalysis. These data provide insights into the evolution of modular templates for donor and acceptor recognition among GT-B fold glycosyltransferases in the synthesis of diverse glycan structures in biological systems.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.