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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. 4 — a The phosphorylation state of OsCTR2 in Osers2^d mhz3-1 is similar to mhz3-1. Osers2^d is a gain-of-function mutant of OsERS2. b The phosphorylation state of OsCTR2 in MHZ3-GFP/Osetr2 is similar to Osetr2. Small black arrows indicate OsCTR2-P^super. For a and b, 2-day-old etiolated seedlings were treated with air, 10 μL/L ethylene, or 10 μL/L 1-MCP for 1 hour before sampling. c OsETR2’s elevation of OsCTR2 phosphorylation requires MHZ3. d OsERS2’s elevation of OsCTR2 phosphorylation requires MHZ3. For c and d, the MHZ3 mutation does not affect the protein levels of OsETR2 and OsERS2. Total protein was extracted from 2-day-old etiolated seedlings. The protein content of OsETR2 was determined using an anti-c-Myc antibody, while the phosphorylation state of OsCTR2 was assessed using an anti-OsCTR2 antibody. An unspecific band was utilized as an internal reference. Ratio represents the ratio of OsCTR2-P to OsCTR2, which is set to 1.0 in the wild type (WT). Three independent experiments were repeated with similar results. Uncropped blots in Source Data file.