{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/combined_ion.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/combined_modified_peptide.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/combined_peptide.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/combined_protein.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/T-ALL8_untreated_r2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/T-ALL8_treated_r2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/T-ALL3_untreated_r2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/T-ALL3_treated_r1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/T-ALL8_treated_r1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/T-ALL8_untreated_r1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/T-ALL3_treated_r2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065179/T-ALL3_untreated_r1.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["caner.saygin@bsd.uchicago.edu"],"submitter":["Diren Arda Karaoglu"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Acute Leukemia"],"software":[""],"submitter_keywords":["Acute leukemia","Menin inhibiton","T-all"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065179"],"tissue":["Leukocyte","Blood"],"sample_protocol":["Samples were lysed using 1X S-Trap lysis buffer (5% SDS, 50 mM TEAB, pH adjusted to 7.55 using 12% phosphoric acid) with protease and phosphatase inhibitors (Thermo Scientific, cat. no. 78442) and bead beat to shear the DNAs. Protein concentration was measured using the BCA assay. The samples (1 mg proteins) were then reduced with TCEP (20mM final) for 30min at 65°C and alkylated with 80 mM iodoacetamide (IAA) in the dark for 30 min at room temperature. Samples were acidified using 12% phosphoric acid (final concentration 1.2%) and diluted using 6x volume of S-Trap binding buffer (methanol containing 100 mM TEAB, pH adjusted to 7.2 using 12% phosphoric acid). Diluted samples were loaded onto an S-Trap midi column (Protifi). Finally, SDS was completely removed from the sample by washing the filter four times with 500 μL of S-Trap binding buffer. Pure protein samples on the filter were then digested using 100 μg of trypsin/Lys-C (#V5073, Promega; 1:20 weight to weight ratio) in 50 mM ammonium bicarbonate, 0.5 mM CaCl2 at 37 °C overnight. Digested peptides were collected by washing the filter in three steps with 400 μL of 50 mM ammonium bicarbonate, pH 8.5, 400 μL of 0.15% formic acid, and 400μL of 0.15% formic acid in 60% acetonitrile. Eluate was dried in vacuo and stored at −80 °C prior to analysis.   For wholeproteome, 5% of the sample was retained and the remaining samples were used for phosphoenrichment.  The peptides were reconstituted in 6% TFA, 40% ACN, and incubated with TiO₂ beads (Titansphere, GL Sciences) pre-equilibrated in 3% DHB in 80% ACN, 6% TFA. A ~5:1 bead-to-peptide ratio was used. The beads were washed sequentially with 6% TFA in 10% and 40% ACN, then loaded onto activated C8 StageTips. Beads were further washed with 6% TFA in 60% ACN and eluted with 5% NH₄OH followed by 10% NH₄OH in 25% ACN. Eluates were dried, resuspended in 1% TFA in 5% ACN, desalted, and eluted with 40% and 60% ACN in 0.1% TFA. Final samples were dried and reconstituted in 0.1% TFA, 4% ACN prior to LC-MS/MS analysis. Mass spectrometry was performed on an Orbitrap Exploris 480 instrument (Thermo Fisher Scientific)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw mass spectrometry data files (.raw) were acquired on the Orbitrap Exploris 480 (Thermo Fisher Scientific) in data-dependent acquisition (DDA) mode. Files were processed using FragPipe, with MSFragger used for database searching against the human UniProt reference proteome and Philosopher for peptide and protein validation and quantification. For whole proteomics analysis, data normalization, imputation and differential group comparisons were performed using MSstats. For phosphoproteomics analysis, data normalization, imputation, and differential group comparisons were performed using PhosR."],"omics_type":["Proteomics"],"labhead":["Caner Saygin"],"instrument_platform":[""],"labhead_affiliation":["Caner Saygin, MD  Assistant Professor of Medicine  Committee on Cancer Biology The University of Chicago"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["ardakaraoglu96@gmail.com"],"publication":["41778833 Shimamoto K, Karaoglu DA, Arnold O, Dhar A, Chan Z, Giordano G, Cheng JX, Youshanlouei HR, Patel AA, DuVall AS, Drazer MW, Kessler L, Burrows F, Odenike O, Thirman MJ, Stock W, Saygin C. Targeting menin in T-lineage acute lymphoblastic leukemia. Mol Cancer Ther. 2026 10.1158/1535-7163.mct-25-0969"],"submitter_affiliation":["The University of Chicago"],"submitter_country":["United States"],"pubmed_abstract":["T-lineage acute lymphoblastic leukemia (T-ALL) lacks effective targeted therapies, with poor outcomes in relapsed/refractory disease. HOXA-high T-ALL is biologically aggressive and often resistant to standard therapy. Menin inhibitors, recently approved for KMT2A-rearranged leukemias, may be effective in T-ALL, but biomarkers of response remain undefined. This study aims to evaluate the efficacy of menin inhibition in T-ALL and identify molecular predictors of sensitivity. We tested menin inhibitors (ziftomenib, revumenib, VTP-50469) in 14 primary T-ALL samples and 8 cell lines, representing HOXA-high and HOXA-low genotypes. In vitro sensitivity assays, xenograft mouse models, transcriptomics, proteomics, and phosphoproteomics were used to characterize drug response. MEF2C modulation experiments and combination studies with CDK1/2 and ERK1/2 inhibitors were performed in vitro and in vivo. Menin inhibitors suppressed leukemic growth in a subset of HOXA-high and HOXA-low primary human T-ALL samples. Similarly, ziftomenib was effective in reducing tumor burden in xenografts without major toxicity. Upon treatment, we observed down-regulation of canonical menin targets (HOXA, MEIS1, MEF2C) and upregulation of T-cell differentiation programs. Phosphoproteomic studies identified MEF2C S222 phosphorylation-mediated by CDK1/2 and ERK1/2-as a predictor of ziftomenib sensitivity in T-ALL. MEF2C overexpression promoted proliferation and ziftomenib resistance, while knockdown impaired growth. Ziftomenib synergized with CDK1/2 and ERK1/2 inhibitors in vitro and improved survival in xenografted mice. In conclusion, a subset of T-ALL, defined by high p-MEF2C S222, is sensitive to menin inhibition. Combining ziftomenib with CDK or ERK inhibition offers synergistic efficacy, supporting biomarker-driven clinical trials of this strategy in relapsed/refractory T-ALL."],"pubmed_title":["Targeting menin in T-lineage acute lymphoblastic leukemia."],"pubmed_authors":["Shimamoto Kathryn K, Karaoglu Diren Arda DA, Arnold Olivia O, Dhar Arjun A, Chan Zachary Z, Giordano Giorgia G, Cheng Jason X JX, Youshanlouei Hamed R HR, Patel Anand A AA, DuVall Adam S AS, Drazer Michael W MW, Kessler Linda L, Burrows Francis F, Odenike Olatoyosi O, Thirman Michael J MJ, Stock Wendy W, Saygin Caner C"],"additional_accession":[]},"is_claimable":false,"name":"Targeting Menin in T-Lineage Acute Lymphoblastic Leukemia","description":"The efficacy of menin inhibition was evaluated in 14 primary T-ALL samples with diverse genetic backgrounds using ziftomenib. Sensitivity was not correlated with HOXA expression or KMT2A rearrangements, and in vivo treatment significantly reduced tumor burden in xenograft models without notable toxicity. Transcriptomic and proteomic analyses confirmed on-target activity, including downregulation of menin targets and activation of differentiation pathways. Phosphoproteomic profiling identified phospho-MEF2C (S222) as a key marker of sensitivity, regulated by CDK and MAPK signaling. Combination treatment with ziftomenib and CDK1/2 or ERK1/2 inhibitors showed synergistic effects, suggesting a mechanistic link between menin inhibition and p-MEF2C–driven T-ALL 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