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. 2021 Oct 8;28(10):835–846. doi: 10.1038/s41594-021-00666-7

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© The Author(s) 2021

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, Ribbon diagram of eIF2α from the pre-dephosphorylation complex (this study, left) and a pre-phosphorylation complex with PKR (PDB 2A19, right). Residues contacting the respective enzymes are highlighted. pSer51, shown on the right, was unresolved in PDB 2A19. b, Coomassie-stained PhosTag gels of wild type and the indicated eIF2α^P mutants (at 2 µM), following dephosphorylation in vitro with PPP1R15A holophosphatases (upper panel). Time-dependent progression of the dephosphorylation reactions above. The dotted line is fit to a first-order decay (of replicates) (middle panel). Best fit of three independent experiments in the ‘upper panel’ ±95% confidence intervals of the k_cat/K_m of the indicated enzyme/substrate pairing in reactions lacking (apo) and containing (holo) G-actin (lower panel). Shown are representative example of experiments reproduced at least three times. c, As in b but reporting on the phosphorylation of the wild type and the indicated eIF2α⁰ mutants (at 2 µM) by the indicated concentration of the kinase PERK. Source data for b and c are available online.

Source data