ArticleNature communications2025
Mechanism of cooperative strigolactone perception by the MAX2 ubiquitin ligase-receptor-substrate complex.
Article in Nature communications, 2025. 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.
- Beyond prediction: Why experimental structural biology remains essential in plants.Current opinion in plant biology · 2026Review
- Negative feedback regulation of karrikin signaling inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Orobanche cumana KAI2d2 mediates the perception of dehydrocostus lactone and strigolactones and is inhibited by triazole ureas.Plant communications · 2026Article
- MAX3 deficiency recruits protective Pseudomonas via modulating the SL-ABA-flavonoid axis to suppress soil-borne pathogen infection.Nature communications · 2026Article
- Divergent strigolactones or karrikins signaling is mediated by preferred AtD14/KAI2-MAX2-SMXL complex targeting specific SMXL domains.iScience · 2026Article
- Genome-Wide Identification and Characterization of theInternational journal of molecular sciences · 2026Article
- Mapping Strigolactone Hydrolysis in DWARF14 via QM/MM String Method.bioRxiv : the preprint server for biology · 2026Article
- Arabidopsis response to the apocarotenoid zaxinone involves interference with strigolactone signaling via binding to DWARF14.Nature communications · 2025Article
- An N-terminal domain specifies developmental control by the SMAX1-LIKE family of transcriptional regulators inProceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Strigolactones are plant hormones that regulate development and mediate interactions with soil organisms, including the germination of parasitic plants such as Striga hermonthica. Strigolactone perception by receptors initiates the degradation of transcriptional repressors via E3 ubiquitin ligases, but the mechanistic link between hormone binding and substrate ubiquitination has remained unclear. We determine cryogenic electron microscopy structures of the receptor-ligase-substrate complex, composed of Arabidopsis ASK1 and substrate, and Striga F-box and receptor proteins. Strigolactone hydrolysis by the receptor, which covalently retains the D-ring, is a prerequisite for complex formation. The substrate engages the complex through two domains, forming a dynamic interface that stabilises the receptor-ligase assembly and repositions the ASK1, suggesting a mechanism for efficient ubiquitination. Here, we show how dynamic, multivalent interactions within the receptor-ligase-substrate complex translate hormone perception into targeted protein degradation, providing insight into how plants integrate hormonal signals into developmental decisions.
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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 OpenQuestion graph.