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. 2023 Sep 21;25(10):1535–1545. doi: 10.1038/s41556-023-01229-2

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© The Author(s) 2023, corrected publication 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. 7 — a–c, Schematic representation of the experimental strategy: a lentiviral GPS library of peptides substrates was generated through microarray oligonucleotide synthesis, wherein the same 540 ORFs exhibiting the greatest degree of stabilization upon MLN4924 treatment were expressed as a series of overlapping 24-mer tiles (a); comparative stability profiling in the presence and absence of MLN4924 then identified GFP–peptide fusions which were targeted by CRLs (b); and for the peptide substrates which exhibited the largest degree of stabilization, saturation mutagenesis was performed to quantify the stability of a panel of mutants in which each residue was mutated to all other possible residues, thereby defining degron motifs at amino acid resolution (c). d–g, Example degron motifs targeted by Cullin-RING E3 ligases. Saturation mutagenesis results for substrates derived from the C-terminus of ALKBH7 (d) and internal peptides derived from ESRRA (e), MATN2 (f) and TOR1AIP2 (g) are shown. Source numerical data are available in Supplementary Tables 18 and 19.