ArticleScientific reports2019
Soluble and membrane-bound protein carrier mediate direct copper transport to the ethylene receptor family.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- Network ontology transcript annotation identifies genetic signals underlying sex determination.Scientific reports · 2026Article
- Integrative approaches for the structure-based functional understanding of the ethylene response in plants.The Plant journal : for cell and molecular biology · 2026Review
- POLARIS is a copper-binding peptide that interacts with ETR1 to negatively regulate ethylene signaling in Arabidopsis.Plant communications · 2025Article
- Molecular mechanism and structural models of protein-mediated copper transfer to the Arabidopsis thaliana ethylene receptor ETR1 at the ER membrane.Scientific reports · 2025Article
- Deciphering Ethylene Signaling via Protein-Protein Interaction in Tomato Fruit.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Structure and dimerization properties of the plant-specific copper chaperone CCH.Scientific reports · 2024Article
- Small Molecules with Thiourea Skeleton Induce Ethylene Response inInternational journal of molecular sciences · 2023Article
- Mapping the helix arrangement of the reconstituted ETR1 ethylene receptor transmembrane domain by EPR spectroscopy.RSC advances · 2022Article
- Ethylene signaling in plants.The Journal of biological chemistry · 2020Review
- Novel insights into the transfer routes of the essential copper cofactor to the ethylene plant hormone receptor family.Plant signaling & behavior · 2020Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The plant hormone ethylene is a key regulator of plant growth, development and stress adaption. Ethylene perception and response are mediated by a family of integral membrane receptors (ETRs) localized at the ER-Golgi network. The biological function of these receptors relies on a protein-bound copper cofactor. Nonetheless, molecular processes and structures controlling assembly and integration of the metal into the functional plant hormone receptor are still unknown. Here, we have explored the molecular pathways of copper transfer from the plant cytosol to the ethylene receptor family by analyzing protein-protein interactions of receptors with soluble and membrane-bound plant copper carriers. Our results suggest that receptors primarily acquire their metal cofactor from copper transporter RESPONSIVE-TO-ANTAGONIST-1 (RAN1) which has been loaded with the transition metal beforehand by soluble copper carriers of the ATX1-family. In addition, we found evidence for a direct interaction of ETRs with soluble chaperones ANTIOXIDANT-1 (ATX1) and COPPER TRANSPORT PROTEIN (CCH) raising the possibility of a direct copper exchange between soluble chaperones and receptors.
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