ArticleNature communications2023
Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Structural insights into proteolysis-dependent and -independent suppression of the master regulator DELLA by the gibberellin receptor.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- 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
- From Fringe to the Mainstream: How ETD MS Brought O-GlcNAc to the Masses.Molecular & cellular proteomics : MCP · 2024Review
- Candidate genes involved in biosynthesis and degradation of the main extracellular matrix polysaccharides of brown algae and their probable evolutionary history.BMC genomics · 2024Article
- In silico simulation of glycosylation and related pathways.Analytical and bioanalytical chemistry · 2024Review
- 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
- Diversity and features of proteins with structural repeats.Biophysical reviews · 2023Review
Corrections and comments
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Authors and funding
15 authors at 4 institutions in 1 country.
Funding
Abstract
SPINDLY (SPY) in Arabidopsis thaliana is a novel nucleocytoplasmic protein O-fucosyltransferase (POFUT), which regulates diverse developmental processes. Sequence analysis indicates that SPY is distinct from ER-localized POFUTs and contains N-terminal tetratricopeptide repeats (TPRs) and a C-terminal catalytic domain resembling the O-linked-N-acetylglucosamine (GlcNAc) transferases (OGTs). However, the structural feature that determines the distinct enzymatic selectivity of SPY remains unknown. Here we report the cryo-electron microscopy (cryo-EM) structure of SPY and its complex with GDP-fucose, revealing distinct active-site features enabling GDP-fucose instead of UDP-GlcNAc binding. SPY forms an antiparallel dimer instead of the X-shaped dimer in human OGT, and its catalytic domain interconverts among multiple conformations. Analysis of mass spectrometry, co-IP, fucosylation activity, and cryo-EM data further demonstrates that the N-terminal disordered peptide in SPY contains trans auto-fucosylation sites and inhibits the POFUT activity, whereas TPRs 1-5 dynamically regulate SPY activity by interfering with protein substrate binding.
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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.