ArticleProceedings of the National Academy of Sciences of the United States of America2016
O-fucosylated glycoproteins form assemblies in close proximity to the nuclear pore complexes of Toxoplasma gondii.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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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.
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Who cites it
37 citing papers in PubMed, 47 citations in OpenAlex.
- Mass Spectrometry-Based Proteomics Methods for Systematic Identification and Quantification of Protein O-Glycosylation in Complex Biological Samples.Journal of the American Society for Mass Spectrometry · 2026Review
- O-fucosylation affects abundance but not localization of select nucleocytoplasmic proteins in toxoplasma gondii.Glycobiology · 2025Article
- A tale of two sugars: O-GlcNAc and O-fucose orchestrate growth, development, and acclimation in plants.Trends in biochemical sciences · 2025Review
- Novel antibodies detect nucleocytoplasmic O-fucose in protist pathogens, cellular slime molds, and plants.mSphere · 2025Article
- Low fucosylation defines the glycocalyx of progenitor cells and melanocytes in the human limbal stem cell niche.Stem cell reports · 2025Article
- Novel antibodies detect nucleocytoplasmic O-fucose in protist pathogens, cellular slime molds, and plants.bioRxiv : the preprint server for biology · 2024Article
- N-acetylglucosamine supplementation fails to bypass the critical acetylation of glucosamine-6-phosphate required for Toxoplasma gondii replication and invasion.PLoS pathogens · 2024Article
- Collision-Induced Dissociation of Fucose and Identification of Anomericity.The journal of physical chemistry. A · 2024Article
- SPINDLY mediates O-fucosylation of hundreds of proteins and sugar-dependent growth in Arabidopsis.The Plant cell · 2023Article
- Sugar and SPY(ce): Large-scale identification of SPINDLY-dependent O-fucosylation targets in Arabidopsis.The Plant cell · 2023Article
- Spindly is a nucleocytosolic O-fucosyltransferase in Dictyostelium and related proteins are widespread in protists and bacteria.Glycobiology · 2023Article
- Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY.Nature communications · 2023Article
- SPINDLY O-fucosylates nuclear and cytoplasmic proteins involved in diverse cellular processes in plants.Plant physiology · 2023Article
- Article
- Not your Mother's MAPKs: Apicomplexan MAPK function in daughter cell budding.PLoS pathogens · 2022Review
- Dual Transcriptomics To Determine Gamma Interferon-Independent Host Response to Intestinal Cryptosporidium parvum Infection.Infection and immunity · 2022Article
- Article
- Novel nucleocytoplasmic protein O-fucosylation by SPINDLY regulates diverse developmental processes in plants.Current opinion in structural biology · 2021Review
- Glycomics, Glycoproteomics, and Glycogenomics: An Inter-Taxa Evolutionary Perspective.Molecular & cellular proteomics : MCP · 2021Review
- The Modular Circuitry of Apicomplexan Cell Division Plasticity.Frontiers in cellular and infection microbiology · 2021Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Toxoplasma gondii is an intracellular parasite that causes disseminated infections in fetuses and immunocompromised individuals. Although gene regulation is important for parasite differentiation and pathogenesis, little is known about protein organization in the nucleus. Here we show that the fucose-binding Aleuria aurantia lectin (AAL) binds to numerous punctate structures in the nuclei of tachyzoites, bradyzoites, and sporozoites but not oocysts. AAL also binds to Hammondia and Neospora nuclei but not to more distantly related apicomplexans. Analyses of the AAL-enriched fraction indicate that AAL binds O-linked fucose added to Ser/Thr residues present in or adjacent to Ser-rich domains (SRDs). Sixty-nine Ser-rich proteins were reproducibly enriched with AAL, including nucleoporins, mRNA-processing enzymes, and cell-signaling proteins. Two endogenous SRDs-containing proteins and an SRD-YFP fusion localize with AAL to the nuclear membrane. Superresolution microscopy showed that the majority of the AAL signal localizes in proximity to nuclear pore complexes. Host cells modify secreted proteins with O-fucose; here we describe the O-fucosylation pathway in the nucleocytosol of a eukaryote. Furthermore, these results suggest O-fucosylation is a mechanism by which proteins involved in gene expression accumulate near the NPC.
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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.