ArticleScientific reports2016
Structural basis of unique ligand specificity of KAI2-like protein from parasitic weed Striga hermonthica.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 55 citations in OpenAlex.
- Negative feedback regulation of karrikin signaling inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Molecular insights into volatile organic compound sensing and signaling in plants.The Plant journal : for cell and molecular biology · 2026Review
- The Multifaceted Impact of Karrikin Signaling in Plants.International journal of molecular sciences · 2025Review
- Role of Strigolactones in the Host Specificity of Broomrapes and Witchweeds.Plant & cell physiology · 2023Review
- A KARRIKIN INSENSITIVE2 paralog in lettuce mediates highly sensitive germination responses to karrikinolide.Plant physiology · 2022Article
- Crystal structure ofPlant direct · 2022Article
- KARRIKIN UP-REGULATED F-BOX 1 (KUF1) imposes negative feedback regulation of karrikin and KAI2 ligand metabolism inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Rational design of Striga hermonthica-specific seed germination inhibitors.Plant physiology · 2022Article
- Masks Start to Drop: Suppressor of MAX2 1-Like Proteins Reveal Their Many Faces.Frontiers in plant science · 2022Review
- The mechanism of host-induced germination in root parasitic plants.Plant physiology · 2021Review
- Article
- Lotus japonicus karrikin receptors display divergent ligand-binding specificities and organ-dependent redundancy.PLoS genetics · 2020Article
- Structure-Function Analysis of SMAX1 Reveals Domains That Mediate Its Karrikin-Induced Proteolysis and Interaction with the Receptor KAI2.The Plant cell · 2020Article
- Strigolactone and Karrikin Signaling Pathways Elicit Ubiquitination and Proteolysis of SMXL2 to Regulate Hypocotyl Elongation in Arabidopsis.The Plant cell · 2020Article
- The Many Models of Strigolactone Signaling.Trends in plant science · 2020Review
- Perception of karrikins by plants: a continuing enigma.Journal of experimental botany · 2020Review
- Divergent receptor proteins confer responses to different karrikins in two ephemeral weeds.Nature communications · 2020Article
- Molecular basis of strigolactone perception in root-parasitic plants: aiming to control its germination with strigolactone agonists/antagonists.Cellular and molecular life sciences : CMLS · 2020Review
- Structural analysis of HTL and D14 proteins reveals the basis for ligand selectivity in Striga.Nature communications · 2018Article
- A missense allele of KARRIKIN-INSENSITIVE2 impairs ligand-binding and downstream signaling in Arabidopsis thaliana.Journal of experimental botany · 2018Article
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The perception of two plant germination inducers, karrikins and strigolactones, are mediated by the proteins KAI2 and D14. Recently, KAI2-type proteins from parasitic weeds, which are possibly related to seed germination induced by strigolactone, have been classified into three clades characterized by different responses to karrikin/strigolactone. Here we characterized a karrikin-binding protein in Striga (ShKAI2iB) that belongs to intermediate-evolving KAI2 and provided the structural bases for its karrikin-binding specificity. Binding assays showed that ShKAI2iB bound karrikins but not strigolactone, differing from other KAI2 and D14. The crystal structures of ShKAI2iB and ShKAI2iB-karrikin complex revealed obvious structural differences in a helix located at the entry of its ligand-binding cavity. This results in a smaller closed pocket, which is also the major cause of ShKAI2iB's specificity of binding karrikin. Our structural study also revealed that a few non-conserved amino acids led to the distinct ligand-binding profile of ShKAI2iB, suggesting that the evolution of KAI2 resulted in its diverse functions.
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