ArticlePlant physiology2023
SPINDLY O-fucosylates nuclear and cytoplasmic proteins involved in diverse cellular processes in plants.
Article in Plant physiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Linking sugar sensing to immunity in plants through O-glycosylation of immune-signaling kinases.bioRxiv : the preprint server for biology · 2026Article
- O-Fucosyltransferase SPINDLY attenuates auxin-induced fruit growth by inhibiting ARF6/8-coactivator mediator complex interaction in Arabidopsis.Nature communications · 2025Article
- A tale of two sugars: O-GlcNAc and O-fucose orchestrate growth, development, and acclimation in plants.Trends in biochemical sciences · 2025Review
- SPY Interacts With Tubulin and Regulates Abscisic Acid-Induced Stomatal Closure in Arabidopsis.Plant direct · 2025Article
- Novel antibodies detect nucleocytoplasmic O-fucose in protist pathogens, cellular slime molds, and plants.mSphere · 2025Article
- Role of Glycans in Equine Endometrial Cell Uptake of Extracellular Vesicles Derived from Amniotic Mesenchymal Stromal Cells.International journal of molecular sciences · 2025Article
- From Fringe to the Mainstream: How ETD MS Brought O-GlcNAc to the Masses.Molecular & cellular proteomics : MCP · 2024Review
- Novel antibodies detect nucleocytoplasmic O-fucose in protist pathogens, cellular slime molds, and plants.bioRxiv : the preprint server for biology · 2024Article
- Identification of a novel Golgi-localized putative glycosyltransferase protein inPlant biotechnology (Tokyo, Japan) · 2024Article
- Structure-based virtual screening identifies small-molecule inhibitors of O-fucosyltransferase SPINDLY in Arabidopsis.The Plant cell · 2024Article
- Workflow enhancement of TurboID-mediated proximity labeling for SPY signaling network mapping.bioRxiv : the preprint server for biology · 2024Article
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- The master growth regulator DELLA binding to histone H2A is essential for DELLA-mediated global transcription regulation.Nature plants · 2023Article
- Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY.Nature communications · 2023Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
SPINDLY (SPY) is a novel nucleocytoplasmic protein O-fucosyltransferase that regulates target protein activity or stability via O-fucosylation of specific Ser/Thr residues. Previous genetic studies indicate that AtSPY regulates plant development during vegetative and reproductive growth by modulating gibberellin and cytokinin responses. AtSPY also regulates the circadian clock and plant responses to biotic and abiotic stresses. The pleiotropic phenotypes of spy mutants point to the likely role of AtSPY in regulating key proteins functioning in diverse cellular pathways. However, very few AtSPY targets are known. Here, we identified 88 SPY targets from Arabidopsis (Arabidopsis thaliana) and Nicotiana benthamiana via the purification of O-fucosylated peptides using Aleuria aurantia lectin followed by electron transfer dissociation-MS/MS analysis. Most AtSPY targets were nuclear proteins that function in DNA repair, transcription, RNA splicing, and nucleocytoplasmic transport. Cytoplasmic AtSPY targets were involved in microtubule-mediated cell division/growth and protein folding. A comparison with the published O-linked-N-acetylglucosamine (O-GlcNAc) proteome revealed that 30% of AtSPY targets were also O-GlcNAcylated, indicating that these distinct glycosylations could co-regulate many protein functions. This study unveiled the roles of O-fucosylation in modulating many key nuclear and cytoplasmic proteins and provided a valuable resource for elucidating the regulatory mechanisms involved.
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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.