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. 2024 Jul 16;15:5987. doi: 10.1038/s41467-024-50290-4

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 7 — Under air conditions, MHZ3 engages with ethylene receptors, enhancing the phosphorylation of OsCTR2, which is tethered to the endoplasmic reticulum membrane via ethylene receptors. Phosphorylated OsEIN2 becomes inactive, turning off ethylene signaling. Upon exposure to ethylene, the interaction between ethylene receptors and MHZ3 weakens, resulting in reduced attachment of OsCTR2 to the endoplasmic reticulum membrane. Consequently, OsCTR2 undergoes dephosphorylation, prompting MHZ3 to transition and stabilize OsEIN2, activating ethylene signaling. After ethylene removal, MHZ3, ethylene receptors, and OsCTR2 reassemble into protein complexes, facilitating the re-phosphorylation of OsCTR2 and deactivating ethylene signaling. In particular, OsETR2 exerted more pronounced regulation over OsCTR2 phosphorylation compared to OsERS2.