ArticleCellular and molecular bioengineering2016
O-GlcNAc-ylation in the Nuclear Pore Complex.
Article in Cellular and molecular bioengineering, 2016. 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, 28 citations in OpenAlex.
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- Nuclear pore dysfunction and disease: a complex opportunity.Nucleus (Austin, Tex.) · 2024Review
- Rapid and large-scale glycopeptide enrichment strategy based on chemical ligation.National science review · 2024Article
- Protein folding and quality control during nuclear transport.Current opinion in cell biology · 2024Review
- Nucleoporin foci are stress-sensitive condensates dispensable for C. elegans nuclear pore assembly.The EMBO journal · 2023Article
- RNAPII Degradation Factor Def1 Is Required for Development, Stress Response, and Full Virulence ofJournal of fungi (Basel, Switzerland) · 2023Article
- Spatial and temporal proteomics reveals the distinct distributions and dynamics of O-GlcNAcylated proteins.Cell reports · 2022Article
- Truncation of the TPR domain of OGT alters substrate and glycosite selection.Analytical and bioanalytical chemistry · 2021Article
- Regulation of O-Linked N-Acetyl Glucosamine Transferase (OGT) through E6 Stimulation of the Ubiquitin Ligase Activity of E6AP.International journal of molecular sciences · 2021Article
- Hexosamine biosynthetic pathway and O-GlcNAc-processing enzymes regulate daily rhythms in protein O-GlcNAcylation.Nature communications · 2021Article
- Nucleocytoplasmic Transport: Regulatory Mechanisms and the Implications in Neurodegeneration.International journal of molecular sciences · 2021Review
- Huntington disease: new insights into molecular pathogenesis and therapeutic opportunities.Nature reviews. Neurology · 2020Review
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Perturbations in Traffic: Aberrant Nucleocytoplasmic Transport at the Heart of Neurodegeneration.Cells · 2018Article
- Structural basis of O-GlcNAc recognition by mammalian 14-3-3 proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mutant Huntingtin Disrupts the Nuclear Pore Complex.Neuron · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
O-GlcNAc-ylation is the post-translational addition of an O-linked β-N-acetylglucosamine to the serine and threonine residues of thousands of proteins in eukaryotic cells. Specifically, half of the thirty different types of protein components in the nuclear pore complex (NPC) are modified by O-GlcNAc, of which the majority are intrinsically disordered nucleoporins (Nups) containing multiple phenylalanine-glycine (FG) repeats. Moreover, these FG-Nups form a strict selectivity barrier with a high density of O-GlcNAc in the NPC to mediate bidirectional trafficking between the cytoplasm and nucleus. However, the roles that O-GlcNAc plays in the structure and function of the NPC remain obscure. In this review paper, we will discuss the current knowledge of O-GlcNAc-ylated Nups, highlight some new techniques used to probe O-GlcNAc's roles in the nuclear pore, and finally propose a new model for the effect of O-GlcNAc on the NPC's permeability.
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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 OpenQuestion graph.