ArticleThe Journal of biological chemistry2015
Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 44 citations in OpenAlex.
- Ethylene-regulated dimeric ETR1 kinase reveals multi-site EIN2 docking targeted by peptides that delay climacteric ripening.Science advances · 2026Article
- Integrative approaches for the structure-based functional understanding of the ethylene response in plants.The Plant journal : for cell and molecular biology · 2026Review
- Structural dynamics of the plant hormone receptor ETR1 in a native-like membrane environment.FEBS letters · 2025Article
- Crystallization of Ethylene Plant Hormone Receptor-Screening for Structure.Biomolecules · 2024Article
- A Model of the Full-Length Cytokinin Receptor: New Insights and Prospects.International journal of molecular sciences · 2023Article
- Utilizing In Silico Approaches to Investigate the Signaling Pathway's Crucial Function inEvolutionary bioinformatics online · 2023Article
- Spectroscopic and QM/MM studies of the Cu(I) binding site of the plant ethylene receptor ETR1.Biophysical journal · 2022Article
- Mapping the helix arrangement of the reconstituted ETR1 ethylene receptor transmembrane domain by EPR spectroscopy.RSC advances · 2022Article
- An Anecdote on Prospective Protein Targets for Developing Novel Plant Growth Regulators.Molecular biotechnology · 2022Review
- Article
- Ethylene signaling in plants.The Journal of biological chemistry · 2020Review
- Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases.Nature communications · 2020Article
- New Insights into Multistep-Phosphorelay (MSP)/ Two-Component System (TCS) Regulation: Are Plants and Bacteria that Different?Plants (Basel, Switzerland) · 2019Review
- Structural Model of the ETR1 Ethylene Receptor Transmembrane Sensor Domain.Scientific reports · 2019Article
- Modeling of Protein⁻Protein Interactions in Cytokinin Signal Transduction.International journal of molecular sciences · 2019Article
- Molecular Analysis of Protein-Protein Interactions in the Ethylene Pathway in the Different Ethylene Receptor Subfamilies.Frontiers in plant science · 2019Article
- Cytokinin perception in potato: new features of canonical players.Journal of experimental botany · 2018Article
- Recognition motif and mechanism of ripening inhibitory peptides in plant hormone receptor ETR1.Scientific reports · 2018Article
- Rapid cadmium SAD phasing at the standard wavelength (1 Å).Acta crystallographica. Section D, Structural biology · 2017Article
- Perception of the plant hormone ethylene: known-knowns and known-unknowns.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ethylene initiates important aspects of plant growth and development through disulfide-linked receptor dimers located in the endoplasmic reticulum. The receptors feature a small transmembrane, ethylene binding domain followed by a large cytosolic domain, which serves as a scaffold for the assembly of large molecular weight complexes of different ethylene receptors and other cellular participants of the ethylene signaling pathway. Here we report the crystallographic structures of the ethylene receptor 1 (ETR1) catalytic ATP-binding and the ethylene response sensor 1 dimerization histidine phosphotransfer (DHp) domains and the solution structure of the entire cytosolic domain of ETR1, all from Arabidopsis thaliana. The isolated dimeric ethylene response sensor 1 DHp domain is asymmetric, the result of different helical bending angles close to the conserved His residue. The structures of the catalytic ATP-binding, DHp, and receiver domains of ethylene receptors and of a homologous, but dissimilar, GAF domain were refined against experimental small angle x-ray scattering data, leading to a structural model of the entire cytosolic domain of the ethylene receptor 1. The model illustrates that the cytosolic domain is shaped like a dumbbell and that the receiver domain is flexible and assumes a position different from those observed in prokaryotic histidine kinases. Furthermore the cytosolic domain of ETR1 plays a key role, interacting with all other receptors and several participants of the ethylene signaling pathway. Our model, therefore, provides the first step toward a detailed understanding of the molecular mechanics of this important signal transduction process in plants.
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