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. 2023 Jun 19;14:3543. doi: 10.1038/s41467-023-38864-0

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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. 1 — a Representative Coomassie-stained SDS-PAGE gel analysis of the purified PEAK3/14-3-3 complex and b corresponding size exclusion chromatography profile resolved on a Superdex 200 10/300 Increase column. Pink bar on the chromatogram indicates collected fractions. Blue tick on the x-axis represents the elution volume of Bovine γ-globulin (158,000 Da) as a reference for the PEAK3/14-3-3 tetrameric complex (161,801 Da). SDS-PAGE and size exclusion chromatography results are representative of at least 3 independent experiments. c Cartoon schematic of PEAK3 domain structure depicting location of the 14-3-3 binding site. d Sequence logo (Weblogo) demonstrating conservation of the 14-3-3 binding site in PEAK3 across evolution. PEAK3 homolog sequences were collected by BLAST search in the Refseq database and clustered at 80% sequence identity. e Cryo-EM map of the PEAK3/14-3-3 complex colored according to local resolution determined by ResMap. f Structure of the PEAK3/14-3-3 complex and zoomed-in view of PEAK3 N-terminal 14-3-3 consensus binding sites superimposed with the cryo-EM map, demonstrating occupancy of both canonical substrate binding grooves in 14-3-3 by phosphorylated 14-3-3 consensus sequences of PEAK3. PEAK3 pseudokinase domains (PsK and PsK’) are in gray and the resolved regions of the N-terminal PEST linkers are shown in black. SHED domain helices αN1 are in yellow, αJ in pink, αK in blue, and αL in purple. 14-3-3ε is shown in green and 14-3-3β is shown in light green.