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. 2023 Jun 19;14:3542. doi: 10.1038/s41467-023-38869-9

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© The Author(s) 2023

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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Fig. 6 — a Sequential ITC binding studies using purified 14-3-3ɣ and purified CrkII^NSH3 domain and PEAK3^tandem-S69 non-phosphorylated and b PEAK3^tandem-pS69 phosphorylated peptides. b High affinity binding of 14-3-3ɣ to PEAK3^tandem-pS69 peptide reduces the affinity of CrkII^NSH3 binding to the adjacent CrkII motif at the tandem site (negative cooperativity). See Supplementary Fig. 6a–d and Supplementary Data 5 for all ITC data.