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. 2021 Jan 20;12(1):101. doi: 10.1038/s41419-021-03400-9

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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. 2 — A In vitro SUMOylation of PKM2. Recombinant wild type (WT) or K270R mutant His-tagged PKM2 were incubated with recombinant SUMO1 in the presence of purified E1(SAE1/UBA2) and E2(UBC9) with or without SENP1. SUMO1 modification were detected using antibody against PKM2 or SUMO1. K, lysine; R, arinine; E, glutamic acid; M, methionine. B SUMOylated PKM2 peptide identified by MS. Recombinant PKM2 protein was digested by trypsin and subjected to LC-MS/MS for identification. The lysine conjugated with QTGG remnant indicates the SUMOylation site. C WT or K270R mutant (KR) Flag-tagged PKM2 were infected into NB4 cells that endogenous PKM2 were depleted. The SUMO1 modification were measured by IP with anti-PKM2 antibody. D, E Multiple-reaction monitoring mass spectrometry(MRM-MS) analysis of SUMOylated PKM2 in leukemia cell lines (D) and primary samples from patients with AML (E).