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. 2022 Dec 8;8:484. doi: 10.1038/s41420-022-01274-0

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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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Fig. 2 — A Table summarizing the strongest interactors identified by mass spectrometry after SLNF5 immunoprecipitation. For each protein, the log10 values of the label-free quantification intensities (LFQ) in the three replicates of the IgG-IP and SLNF5-IP are reported. B, C Validation of SLFN5 - B55α interaction in U2OS and Jurkat E1.6 cells by co-immunoprecipitation followed by Western blotting. #112/5/6 anti-SLFN5 was used to co-immunoprecipitate endogenous SLFN5 and its interactors. Immunoprecipitation with an irrelevant mouse IgG antibody served as a negative control (control IP). B55α recovery was confirmed using an antibody against the regulatory subunit B55α. UF, unbound fraction. The Western blot shows a representative experiment from three independent validations. D SLFN5 contains a cluster of five TP motifs in the DBD and NTPase domain, and single TP (T143-P144) and SP (S786-P787) motifs at the N-terminus and C-terminus, respectively. E SLFN5 is phosphorylated at T/SP minimal CDK consensus sequences. An anti-pT/SP antibody was used for immunoprecipitation in U2OS cells. The membrane was probed with #112/5/6 anti-SLFN5. Immunoprecipitation with an irrelevant mouse IgG antibody served as a negative control. The Western blot shows a representative experiment from three independent experiments. F SLFN5-DBD TP sites are phosphorylated by Cyclin B-CDK1 and dephosphorylated by PP2A-B55α. Timecourse of SLFN5-DBD dephosphorylation. Comassie staining serves as loading control. The Radiograph shows a representative experiment from three independent experiments.