ArticleThe Journal of biological chemistry2015
Loss of α1,6-Fucosyltransferase Decreases Hippocampal Long Term Potentiation: IMPLICATIONS FOR CORE FUCOSYLATION IN THE REGULATION OF AMPA RECEPTOR HETEROMERIZATION AND CELLULAR SIGNALING.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 53 citations in OpenAlex.
- Glycosylation in gut-brain communication: from the intestinal barrier and microbiota to immune and neural signaling.Gut microbes · 2026Review
- Signal peptide peptidase- and SPP-like 3-dependent shedding of α1,6-fucosyltransferase differentially affects core fucosylation.The Journal of biological chemistry · 2026Article
- L-fucose administration ameliorates chronic social defeat stress-induced depressive-like behaviors by restoring GDP-fucose biosynthetic activation and core fucosylation.Frontiers in immunology · 2026Article
- Roles of Core Fucosylation in Neuroinflammation and Its Possibility for Application.Advances in experimental medicine and biology · 2026Review
- Structure, function, and implications of fucosyltransferases in health and disease.Nature communications · 2025Review
- Roles of core fucosylation modification in immune system and diseases.Cell insight · 2025Review
- Chemoenzymatic Labeling, Detection and Profiling of Core Fucosylation in Live Cells.Journal of the American Chemical Society · 2024Article
- Fucosyltransferase 8 regulates adult neurogenesis and cognition of mice by modulating the Itga6-PI3K/Akt signaling pathway.Science China. Life sciences · 2024Article
- Aberrant glycosylation in schizophrenia: insights into pathophysiological mechanisms and therapeutic potentials.Frontiers in pharmacology · 2024Review
- Changes in tissue proteinPNAS nexus · 2024Article
- Brain N-Glycosylation and Lipidomic Profile Changes Induced by a High-Fat Diet in Dyslipidemic Hamsters.International journal of molecular sciences · 2023Article
- Known and Unexplored Post-Translational Modification Pathways in Schizophrenia.Advances in experimental medicine and biology · 2022Article
- Complete spatial characterisation of N-glycosylation upon striatal neuroinflammation in the rodent brain.Journal of neuroinflammation · 2021Article
- Keratan sulfate-based glycomimetics using Langerin as a target for COPD: lessons from studies on Fut8 and core fucose.Biochemical Society transactions · 2021Review
- Characterizing human α-1,6-fucosyltransferase (FUT8) substrate specificity and structural similarities with related fucosyltransferases.The Journal of biological chemistry · 2020Article
- Sweet Control: MicroRNA Regulation of the Glycome.Biochemistry · 2020Review
- The SH3 domain in the fucosyltransferase FUT8 controls FUT8 activity and localization and is essential for core fucosylation.The Journal of biological chemistry · 2020Article
- Post-translational protein modifications in schizophrenia.NPJ schizophrenia · 2020Review
- 3D Structure and Function of Glycosyltransferases Involved inInternational journal of molecular sciences · 2020Review
- AMPA receptors in the synapse turnover by monomer diffusion.Nature communications · 2019Article
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Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Core fucosylation is catalyzed by α1,6-fucosyltransferase (FUT8), which transfers a fucose residue to the innermost GlcNAc residue via α1,6-linkage on N-glycans in mammals. We previously reported that Fut8-knock-out (Fut8(-/-)) mice showed a schizophrenia-like phenotype and a decrease in working memory. To understand the underlying molecular mechanism, we analyzed early form long term potentiation (E-LTP), which is closely related to learning and memory in the hippocampus. The scale of E-LTP induced by high frequency stimulation was significantly decreased in Fut8(-/-) mice. Tetraethylammonium-induced LTP showed no significant differences, suggesting that the decline in E-LTP was caused by postsynaptic events. Unexpectedly, the phosphorylation levels of calcium/calmodulin-dependent protein kinase II (CaMKII), an important mediator of learning and memory in postsynapses, were greatly increased in Fut8(-/-) mice. The expression levels of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionate receptors (AMPARs) in the postsynaptic density were enhanced in Fut8(-/-) mice, although there were no significant differences in the total expression levels, implicating that AMPARs without core fucosylation might exist in an active state. The activation of AMPARs was further confirmed by Fura-2 calcium imaging using primary cultured neurons. Taken together, loss of core fucosylation on AMPARs enhanced their heteromerization, which increase sensitivity for postsynaptic depolarization and persistently activate N-methyl-d-aspartate receptors as well as Ca(2+) influx and CaMKII and then impair LTP.
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