ArticleNature communications2022
Structural insights into mechanism and specificity of the plant protein O-fucosyltransferase SPINDLY.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- 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
- Novel antibodies detect nucleocytoplasmic O-fucose in protist pathogens, cellular slime molds, and plants.mSphere · 2025Article
- Multiprotein Complexes of Plant Glycosyltransferases Involved in Their Function and Trafficking.Plants (Basel, Switzerland) · 2025Review
- Genetic Variation Analysis and Development of KASP Marker for Leaf Area and Hight in Southern-TypePlants (Basel, Switzerland) · 2025Article
- Novel antibodies detect nucleocytoplasmic O-fucose in protist pathogens, cellular slime molds, and plants.bioRxiv : the preprint server for biology · 2024Article
- Structure-based virtual screening identifies small-molecule inhibitors of O-fucosyltransferase SPINDLY in Arabidopsis.The Plant cell · 2024Article
- Drug repurposing against fucosyltransferase-2 via docking, STD-NMR, and molecular dynamic simulation studies.PloS one · 2024Article
- Analysis of Growth Trajectories and Verification of Related SNPs inInternational journal of molecular sciences · 2023Article
- Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase.Nature communications · 2023Article
- Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY.Nature communications · 2023Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arabidopsis glycosyltransferase family 41 (GT41) protein SPINDLY (SPY) plays pleiotropic roles in plant development. Despite the amino acid sequence is similar to human O-GlcNAc transferase, Arabidopsis SPY has been identified as a novel nucleocytoplasmic protein O-fucosyltransferase. SPY-like proteins extensively exist in diverse organisms, indicating that O-fucosylation by SPY is a common way to regulate intracellular protein functions. However, the details of how SPY recognizes and glycosylates substrates are unknown. Here, we present a crystal structure of Arabidopsis SPY/GDP complex at 2.85 Å resolution. SPY adopts a head-to-tail dimer. Strikingly, the conformation of a 'catalytic SPY'/GDP/'substrate SPY' complex formed by two symmetry-related SPY dimers is captured in the crystal lattice. The structure together with mutagenesis and enzymatic data demonstrate SPY can fucosylate itself and SPY's self-fucosylation region negatively regulates its enzyme activity, reveal SPY's substrate recognition and enzyme mechanism, and provide insights into the glycan donor substrate selection in GT41 proteins.
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