ArticleNature chemical biology2025
FUT10 and FUT11 are protein O-fucosyltransferases that modify protein EMI domains.
Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Multi-omics causal inference of childhood asthma triggered by ambient particulate matter.ERJ open research · 2026Article
- O-mannosylation and furin processing are critical maturation events for the KIAA1549 protein implicated in pediatric pilocytic astrocytomas.The Journal of biological chemistry · 2026Article
- Behind the scenes: how the EMILIN/Multimerin family shapes the cancer landscape.The FEBS journal · 2026Review
- Targeted multiplex gene knockouts in Lemna minor using CRISPR/Cas9.Transgenic research · 2026Article
- L-Fucose: a dietary sugar with multifaceted potential in the biology and therapy of cancer.Nature reviews. Cancer · 2026Review
- Glycan-related genes and genetic disorders.Journal of human genetics · 2026Review
- Fucose metabolism as a central axis linking inflammation, immunity, and cancer in the gut.Frontiers in immunology · 2026Review
- Structure, function, and implications of fucosyltransferases in health and disease.Nature communications · 2025Review
- Light-modulated stem cells in the camera-type eye of an annelid model for adult brain plasticity.Nature communications · 2025Article
- Chemical Strategies to Custom-Modify α(1→3)-Fucosylated Glycan Motifs of the Human Glycocalyx.JACS Au · 2025Review
- Single-cell glycome and transcriptome profiling uncovers the glycan signature of each cell subpopulation of human iPSC-derived neurons.Stem cell reports · 2025Article
- SEC61B regulates calcium flux and platelet hyperreactivity in diabetes.The Journal of clinical investigation · 2025Article
- Review
- Effect of glycosylation on protein folding: From biological roles to chemical protein synthesis.iScience · 2025Review
- ProteinMolecules (Basel, Switzerland) · 2025Review
- Multimeric protein interaction and complex prediction: Structure, dynamics and function.Computational and structural biotechnology journal · 2025Review
Corrections and comments
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Authors and funding
16 authors.
Funding
Abstract
O-Fucosylation plays crucial roles in various essential biological events. Alongside the well-established O-fucosylation of epidermal growth factor-like repeats by protein O-fucosyltransferase 1 (POFUT1) and thrombospondin type 1 repeats by POFUT2, we recently identified a type of O-fucosylation on the elastin microfibril interface (EMI) domain of Multimerin-1 (MMRN1). Here, using AlphaFold2 screens, co-immunoprecipitation, enzymatic assays combined with mass spectrometric analysis and CRISPR-Cas9 knockouts, we demonstrate that FUT10 and FUT11, originally annotated in UniProt as α1,3-fucosyltransferases, are actually POFUTs responsible for modifying EMI domains; thus, we renamed them as POFUT3 and POFUT4, respectively. Like POFUT1/2, POFUT3/4 function in the endoplasmic reticulum, require folded domain structures for modification and participate in a non-canonical endoplasmic reticulum quality control pathway for EMI domain-containing protein secretion. This finding expands the O-fucosylation repertoire and provides an entry point for further exploration in this emerging field of O-fucosylation.
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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 Socratic graph.