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. 2022 Jun 29;609(7926):400–407. doi: 10.1038/s41586-022-04838-3

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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. 9 — a, Representative peptide dephosphorylation assay showing higher catalytic efficiency for PP1C when complexed with SHOC2 and KRAS against A/B/CRAF NTpS, but not against Non-Target Peptides. Data points are from two time points (n = 2). See Fig. 4 for statistical summary of three independent experiments. [PP1C] = 10 nM, [KRAS(GCP)] = 10 µM. b, Peptide dephosphorylation assay showing PP1C (green) or PP1C:SHOC2:KRAS (maroon) dephosphorylation of p-Nitrophenyl Phosphate (PNPP). Error bars represent mean +/- SD of four time points (n = 4). [PP1C] = 10 nM, [KRAS(GCP)] = 10 µM. Results are representative of two independent experiments. c, SEC analysis showing no association between SHOC2:PP1C:KRAS and BRAF kinase domain (orange) (top) with associated SDS-PAGE analysis (bottom). Results representative of two independent experiments d, Sequence alignment of A/B/CRAF NTpS (expected biological targets of SHOC2:PP1C:RAS), CRAF CTpS and Phosphorylase A pS15 (Non-Target Peptides). NTpS peptides contain C terminal hydrophobic residues (yellow) and both NTpS and CTpS contain critical 14-3-3 interacting residues (blue) which may have evolved for 14-3-3 recognition, rather than SHOC2:PP1C:RAS recognition. e, Sequence logo showing conservation among A/B/CRAF NTpS across 18 representative species from C. elegans to H. sapiens (where equivalent RAF isoforms were available) (top), or separate RAF NTpS across species (bottom three). f, SHOC2:PP1C:MRAS structure with PP1C substrate binding grooves highlighted (red ovals).