ArticleThe Journal of cell biology2021
O-GlcNAc modification of nuclear pore complexes accelerates bidirectional transport.
Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 36 citations in OpenAlex.
- The responsive nucleus: morphological signatures of cellular state.Nucleus (Austin, Tex.) · 2026Review
- Sweetening the bonds: how O-GlcNAcylation modulates cell adhesion.Acta pharmacologica Sinica · 2026Review
- Expandable DNA-origami rings as a nanomechanical platform for studying disordered nucleoporins.bioRxiv : the preprint server for biology · 2026Article
- Mechanoresponsive modulation of nuclear pore complex structure and function bybioRxiv : the preprint server for biology · 2026Article
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- Effects of Nanopore Confinement on the Conformational, Dynamical, and Self-Assembly Properties of an FG-Repeat Peptide.The journal of physical chemistry. B · 2025Article
- Effects of Nanopore Confinement on the Conformational, Dynamical, and Self-Assembly Properties of an FG-Repeat Peptide.bioRxiv : the preprint server for biology · 2025Article
- Zscan4 as a Candidate Conveyor of Early Developmental Defects in O-GlcNAc Transferase Intellectual Disability.Molecular & cellular proteomics : MCP · 2025Article
- O-fucosylation affects abundance but not localization of select nucleocytoplasmic proteins in toxoplasma gondii.Glycobiology · 2025Article
- Episodic transport of protein aggregates achieves a positive size selectivity in aggresome formation.Nature communications · 2025Article
- O-GlcNAc modulation of nuclear pore complexes orchestrates mRNA export efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A tale of two sugars: O-GlcNAc and O-fucose orchestrate growth, development, and acclimation in plants.Trends in biochemical sciences · 2025Review
- Nuclear pore dysfunction and disease: a complex opportunity.Nucleus (Austin, Tex.) · 2024Review
- Protein folding and quality control during nuclear transport.Current opinion in cell biology · 2024Review
- Workflow enhancement of TurboID-mediated proximity labeling for SPY signaling network mapping.bioRxiv : the preprint server for biology · 2024Article
- Quantitative comparison of nuclear transport inhibition by SARS coronavirus ORF6 reveals the importance of oligomerization.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Current Technologies Unraveling the Significance of Post-Translational Modifications (PTMs) as Crucial Players in Neurodegeneration.Biomolecules · 2024Review
- Understanding and exploiting the roles of O-GlcNAc in neurodegenerative diseases.The Journal of biological chemistry · 2023Review
- Systematic analysis of the impact of phosphorylation and O-GlcNAcylation on protein subcellular localization.Cell reports · 2023Article
- Nucleoporin foci are stress-sensitive condensates dispensable for C. elegans nuclear pore assembly.The EMBO journal · 2023Article
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2 authors at 1 institution in 1 country.
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Abstract
Macromolecular transport across the nuclear envelope depends on facilitated diffusion through nuclear pore complexes (NPCs). The interior of NPCs contains a permeability barrier made of phenylalanine-glycine (FG) repeat domains that selectively facilitates the permeation of cargoes bound to nuclear transport receptors (NTRs). FG-repeat domains in NPCs are a major site of O-linked N-acetylglucosamine (O-GlcNAc) modification, but the functional role of this modification in nucleocytoplasmic transport is unclear. We developed high-throughput assays based on optogenetic probes to quantify the kinetics of nuclear import and export in living human cells. We found that increasing O-GlcNAc modification of the NPC accelerated NTR-facilitated transport of proteins in both directions, and decreasing modification slowed transport. Superresolution imaging revealed strong enrichment of O-GlcNAc at the FG-repeat barrier. O-GlcNAc modification also accelerated passive permeation of a small, inert protein through NPCs. We conclude that O-GlcNAc modification accelerates nucleocytoplasmic transport by enhancing the nonspecific permeability of the FG-repeat barrier, perhaps by steric inhibition of interactions between FG repeats.
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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.