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Protein supernatants were collected, and concentration was measured with the bicinchoninic acid assay (Thermo-Fisher), according to manufacturer’s instructions. A total of 100 µg of protein lysate (per sample) was precipitated in ice-cold (-20ºC) methanol, and were resuspended in 7M Urea in 100mM ammonium bicarbonate buffer (AMBIC), and reduced by adding a tris(2-carboxyethyl)phosphine in 100mM AMBIC and incubating them for 1 h at 37 °C. Alkylation was performed by adding iodoacetamide in AMBIC and incubating them for 30 min in the dark at RT. Urea was then diluted to 1M with AMBIC and Trypsin/Lys-C (Promega) was added in a 1:100 w/w ratio (enzyme/protein) to the samples, which were incubated at 37C for 16hrs under agitation. Formic acid (FA) was then added to acidify the peptide mixtures. Samples were centrifuged at 14,000xg for 20 min at 4C, supernatants were collected, and peptide mixtures were desalted using Peptide desalting spin columns (Thermo Fisher) according to manufacturer instructions. Eluates were dried in speedvac, resuspended in triethil ammonium bicarbonate (TEAB) and peptides were chemically labelled using Tandem Mass Tag 10 (TMT; Thermo Fisher) according to manufacturer instructions. Labelled samples were then pooled and dried.TMT10 pools were fractionated using a Waters XBridge BEH130 C18 (3.5 μm, 2.1 × 150 mm column; Waters) coupled to a Ultimate 3000 system (Thermo). Equilibration and peptide elution buffers were composed of 20mM ammonium formate in high grade water and 10mM ammonium formate in 90% V/V ACN, respectively. Gradient was run as follows (constant flow of 200 μL/min): 3 min at 0% B, 35% B in 94 min, 80% B in 1 min, and 10 min at 80% B. Fractions were collected for the first 97 minutes using a Thermo Scientific fraction collector, for a total of 96 fractions. Of these, 90% of the eluted volume was concatenated into 12 fractions for downstream phosphopeptide enrichment, while the remainder was concatenated in 24 fractions for proteome analysis. Concatenation scheme for the eluates’ 96-well plates was: fraction 1 (well A1, C1, E1, G1), fraction 2 (well A2, C2, E2, G2), etc. Concatenated fractions were dried and frozen until downstream processing or MS analysis. Samples for spectral library preparation (cell line and Allprep flowthrough fractions) and clinical cohort analysis (SCAN-B Allprep flowthroughs) were processed according to a previously published automated phosphopeptide enrichment protocol 1. Briefly, peptide mixtures out of high-pH fractionation or directly out of C18 desalting were loaded on the AssayMAP Bravo platform. The Fe(III)-NTA cartridges employed here were primed with 50% V/V ACN, 0.1% V/V trifluoroacetic acid (TFA), equilibrated with loading buffer (i.e. 80% V/V ACN and 0.1% V/V TFA in high grade water). Peptide mixtures were then loaded on phosphoenrichment cartridges, washed with loading buffer, and eluted with 5% V/V ammonia solution into a 50% V/V FA solution (eluates’ plate). Samples were then dried and stored at -80˚C until MS analysis."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["TMT-pools were analyzed on a Q-Exactive HF-X (Thermo-Fisher) system coupled to a Dionex Ultimate 3000 high performance liquid chromatography system (Thermo-Fisher). Peptides were trapped on a μPAC Neo trap columns and separated on a μPA Neo 50cm column, mobile phases and flow employed in this analysis were the same as above. Peptides were eluted in a 140 min gradient (flow: 400 nL/min; mobile phase A: 0.1% formic acid in H2O; mobile phase B: 100% acetonitrile and 0.1% formic acid). The chromatographic gradient was run as follows: 6% B for 3min; 6-25% B in 110 min; 25-40% B in 10min; 40-99% B in 1min; 99% B for 10 min. The 15 most abundant peaks from the MS scan (resolution: 120,000 at 200 m/z) were selected and fragmented by higher energy induced collision dissociation (HCD; collision energy: 34). Dynamic exclusion was activated (window: 30s) Automatic Gain Control (AGC) target for full MS and MS/MS scans was set to 3E6 and 1E3, respectively. Thermo RAW files were processed through Fragpipe (v22.0; https://fragpipe.nesvilab.org/) with the built-in TMT10 method For the analysis of the phosphoproteome files, the STY option was enabled in the modification tab of the MSFragger panel. FASTA file for database search employed for DDA and DIA searches was downloaded from Uniprot (www.uniprot.org), selecting only the Swissprot subset (version 2024.01.15). Proteome and phosphosite tables were filtered for missing data (MD filter transcriptome: 30%, proteome: 40%; phosphoproteome: 80%) and mean-centered across samples and features (genes, proteins, phosphosites). For the proteomic and phosphoproteomic datasets tables batch effect correction and quantile normalization scripts were performed with limma (v3.46.0) in R (v4.0.5). Pathway analyses were performed with Gene Set Enrichment Analysis (GSEA; v4.1.0) 2 using the Hallmarks and Reactome databases (from MSigdDB, v2024.01). GSEA settings were as follows: gene set permutation type, classic scoring method, t-test metric. False Discovery Rate (FDR) cutoff for significant pathways was set to 0.25. Reactome pathways were plotted using the Enrichment Map plug-in in Cytoscape (v3.8.2). Sample-wise pathway scores were calculated using GSVA 3 (v1.38.2) in R. Phosphoproteomic data was analyzed by Kinase-Substrate Enrichment Analysis (KSEA, v0.99.0) 4 in R. Here, Network KIN terms were allowed with a cutoff of 5. Enriched Kinases were selected based on p-value (< 0.05) and number of substrates (> 2)."],"omics_type":["Proteomics"],"labhead":["Carmela Dell'Aversana"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Universita Della Campania Luigi Vanvitelli"],"species":["Homo Sapiens (human)"],"publication":["41872140 Sgueglia G, Massaro C, Muro A, Lettiero I, D'Agostino E, Favale G, Simonelli N, Del Gaudio N, Carafa V, De Marchi T, Rotili D, Valente S, Mai A, Sbardella G, De Simone M, Altucci L, Dell'Aversana C. Dynamic epigenetic regulation of BCLAF1 splicing in acute myeloid leukemia. Cell Death Dis. 2026 17(1):344 10.1038/s41419-026-08594-4"],"submitter_mail":["tommaso.de_marchi@med.lu.se"],"submitter_affiliation":["Lund University"],"submitter_country":["Sweden"],"pubmed_abstract":["Dysregulation of alternative splicing is increasingly associated with cancer development and tumor progression. BCL2-associated transcription factor 1 (BCLAF1) is involved in a wide range of biological processes and it is continuously being investigated due to its intricate function in tumorigenesis and drug resistance. In acute myeloid leukemia (AML) cell lines, we identified two distinct, unbalanced isoforms of BCLAF1: the full-length isoform, which exhibits oncogenic properties, and the short-length isoform, which seems to act as a tumor suppressor. Treatment with specific epidrugs can re-establish the physiological balance of full- and short-length isoforms, restoring their correct equilibrium. Our results suggest the existence of a newly identified mechanism underlying the regulation of BCLAF1 splicing orchestrated, at least in part, by the interplay between HDAC1 and DNMT3A, and directly correlated with the healthy or cancerous state of hematopoietic cells. Our findings shed light on a novel regulatory axis in AML and highlight the potential of epidrugs to restore normal splicing patterns, paving the way for innovative therapies."],"pubmed_title":["Dynamic epigenetic regulation of BCLAF1 splicing in acute myeloid leukemia."],"pubmed_authors":["Sgueglia Giulia G, Massaro Crescenzo C, Muro Annamaria A, Lettiero Ida I, D'Agostino Erika E, Favale Gregorio G, Simonelli Nicla N, Del Gaudio Nunzio N, Carafa Vincenzo V, De Marchi Tommaso T, Rotili Dante D, Valente Sergio S, Mai Antonello A, Sbardella Gianluca G, De Simone Mariacarla M, Altucci Lucia L, Dell'Aversana Carmela C"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of U937 cells after SAHA treatment","description":"U937 cells were treated with SAHA and DMSO. Proteome and phosphoproteome were measured by TMT10 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