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In brief, nuclear lysates were subjected to SP3-based protein clean-up (ref), and resuspended in ammonium bicarbonate 50mM ahead of tryptic digestion for 18h at 37°C. Peptides were then acidified with 0.1% TFA, and quantified with BCA peptide quantitative assay (Thermo Scientific #23275). 200ng of peptides were then separated on a IonOpticks Aurora 3column in 120min active gradient performed on a nanoElute2 (Bruker Daltonics) coupled to a timsTOF HT (Bruker Daltonics). Data were acquired in diaPASEF mode with 1.1 cycle time."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["RAW data were processed with neural networks based data independent DIANN software (v1.9) (Demichev V 2020).. FDR was set to 1% at both protein and peptide levels. Match between runs option was enabled,. For further protein analysis, Perseus software was used ( Tyanova, S 2016. Two-sided t-test statistics were used for the generation of the volcano plots based on intensity log10 values of expressed proteins. FDR was 0.05 and S0 constant was 0.1. Pathway enrichment analysis was done using the Metascape resource (Zhou Y 2019)."],"omics_type":["Proteomics"],"labhead":["Ali Bakr"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["German Cancer Research Center (DKFZ), Division of Cancer Epigenomics"],"species":["Homo Sapiens (human)"],"publication":["41735198 Corte GD, Eldesouky H, Puchan J, Öz S, Everatt E, Goyal A, Sigismondo G, Oppermann U, Plass C, Weichenhan D, Bakr A. ID3 deficiency alters chromatin accessibility at DSB sites and enhances vulnerability to HDAC inhibition. Int J Cancer. 2026 158(12):3173-3186 10.1002/ijc.70400"],"submitter_mail":["gianluca.sigismondo@gmail.com"],"submitter_affiliation":["DKFZ"],"submitter_country":["Germany"],"pubmed_abstract":["The inhibitor of DNA-binding 3 (ID3) plays a crucial role in DNA double-strand break (DSB) repair. We previously reported that ID3 loss reduced chromatin accessibility at DNA repair gene promoters, yet its exact role in DNA repair via chromatin regulation remains elusive. Using the AID-DIvA cell system with inducible DSBs, we show that ID3 directly regulates chromatin accessibility at DSB sites, as demonstrated by reduced chromatin accessibility and lower H3K27ac levels in ID3-knockout (KO) cells. Loss of ID3 renders cells susceptible to histone deacetylase (HDAC) inhibition, particularly to the Class I HDAC inhibitor, leading to the accumulation of unrepaired DSBs and delayed cell cycle progression. Transcriptome and proteome analyses revealed that HDAC inhibition in ID3-KO cells results in the downregulation of gene sets involved in the regulation of cell cycle and cell division. The synthetic lethality observed between ID3 loss and Class I HDAC inhibition underscores a novel therapeutic vulnerability in ID3-deficient cancers, driven by compounded defects in chromatin remodeling, cell cycle, and DNA repair. Our study provides new insights into the relationship between chromatin regulation and genome stability, with implications for targeted cancer therapies."],"pubmed_title":["ID3 deficiency alters chromatin accessibility at DSB sites and enhances vulnerability to HDAC inhibition."],"pubmed_authors":["Corte Giuditta Della GD, Eldesouky Hossam H, Puchan Julia J, Öz Sercan S, Everatt Elena E, Goyal Ashish A, Sigismondo Gianluca G, Oppermann Udo U, Plass Christoph C, Weichenhan Dieter D, Bakr Ali A"],"additional_accession":[]},"is_claimable":false,"name":"ID3 Deficiency Alters Chromatin Accessibility at DSB Sites and Enhances Vulnerability to HDAC Inhibition","description":"The inhibitor of DNA-binding 3 (ID3) plays a crucial role in DNA double-strand break (DSB) repair. We previously reported that ID3 loss reduced chromatin accessibility at DNA repair gene promoters, yet its exact role in DNA repair via chromatin regulation remained elusive. Using the AID-DIvA cell system with inducible DSBs, we show that ID3 directly regulates chromatin accessibility at DSB sites, as demonstrated by reduced chromatin accessibility and lower H3K27ac levels in ID3-knockout (KO) cells. Loss of ID3 renders cells highly sensitive to histone deacetylase (HDAC) inhibition, particularly to the Class I HDAC inhibitor, leading to the accumulation of unrepaired DSBs and delayed cell cycle progression. Transcriptome and proteome analyses revealed that HDAC inhibition in ID3-KO cells results in the downregulation of gene sets involved in the regulation of cell cycle and cell division. The synthetic lethality observed between ID3 loss and Class I HDAC inhibition underscores a novel therapeutic vulnerability in ID3-deficient cancers, driven by compounded defects in chromatin remodeling, cell cycle, and DNA repair. Our study provides new insights into the relationship between chromatin regulation and genome stability, with implications for targeted cancer 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