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. 2022 Aug 2;609(7927):611–615. doi: 10.1038/s41586-022-05143-9

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© The Author(s) 2022

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Extended Data Fig. 7 — a, The binding affinity between PIN1 and IBA, IPA, or 4-Cl-IAA under pH 7.0 or 5.5 as examined by SPR, respectively. Under acidic pH, the binding affinities decreased dramatically for IBA and IPA, while for 4-Cl-IAA, the K_d had an about two-fold increase. These results suggest that PINs can bind range of natural auxins but whether PIN1 can transport these auxins awaits further studies. b, IAA-ITC results for the WT PIN1 at pH 5.5. c–f, IAA-ITC results for the PIN1 V51A, N112A, I582A and Y145A mutants at pH 7.0, respectively. No apparent binding are derived for the N112A, I582A and Y145A mutants. For V51A, the fitted binding affinity is 1.39 ± 0.16 mM, 17-fold higher than that of the WT PIN1. g, h, NPA-ITC results for the PIN1 N112A and Y145A mutants. i, Cartoon model for the alternating access mechanism of IAA transport by PIN1 and inhibition by NPA.