ArticleNature communications2024
Structural insights into strigolactone catabolism by carboxylesterases reveal a conserved conformational regulation.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Negative feedback regulation of karrikin signaling inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Strigolactones in Plant Abiotic Stress Resilience: Hormonal Crosstalk, Mechanistic Regulation, and Agricultural Prospects.Plants (Basel, Switzerland) · 2026Review
- Salicylic acid modulates its catabolic enzymes via proteasomal degradation linked to SCF-associated proximity networks.Nature communications · 2026Article
- Axially engineered single atoms in enzyme-mimic-binding pocket steering dehalogenation-polymerization pathways toward water pollutant upcycling.Nature communications · 2026Article
- Molecular Basis for Catalysis and Regulation of the Strigolactone Catabolic Enzyme CXE15.Nature communications · 2025Article
- Strigolactones coordinate barley tillering and grain size.Journal of experimental botany · 2025Article
- Beyond static structures: protein dynamic conformations modeling in the post-AlphaFold era.Briefings in bioinformatics · 2025Review
- Dissecting genomic regions and candidate genes for pod borer resistance and component traits in pigeonpea minicore collection.Frontiers in plant science · 2025Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Phytohormone levels are regulated through specialized enzymes, participating not only in their biosynthesis but also in post-signaling processes for signal inactivation and cue depletion. Arabidopsis thaliana (At) carboxylesterase 15 (CXE15) and carboxylesterase 20 (CXE20) have been shown to deplete strigolactones (SLs) that coordinate various growth and developmental processes and function as signaling molecules in the rhizosphere. Here, we elucidate the X-ray crystal structures of AtCXE15 (both apo and SL intermediate bound) and AtCXE20, revealing insights into the mechanisms of SL binding and catabolism. The N-terminal regions of CXE15 and CXE20 exhibit distinct secondary structures, with CXE15 characterized by an alpha helix and CXE20 by an alpha/beta fold. These structural differences play pivotal roles in regulating variable SL hydrolysis rates. Our findings, both in vitro and in planta, indicate that a transition of the N-terminal helix domain of CXE15 between open and closed forms facilitates robust SL hydrolysis. The results not only illuminate the distinctive process of phytohormone breakdown but also uncover a molecular architecture and mode of plasticity within a specific class of carboxylesterases.
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