Prideapplication/xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/proteinGroups.txtftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/IP-MS-SampleInfo_MOLM13_EO241-EO252.txtftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/mqpar_2.xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/EO251.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/EO242.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/EO247.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/EO245.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/EO243.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/EO248.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/EO250.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/EO252.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/EO241.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/EO246.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/EO249.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067825/EO244.rawprimaryOK200m.timmers@dkfz-heidelberg.deMarc TimmersAffinity purification coupled with mass spectrometry proteomicsMass SpectrometryjundMenin; jund; chromatin modifiers; epigenetic; mllr leukemia; vtp-50469epigeneticMeninvtp-50469mllr leukemiachromatin modifiershttps://www.ebi.ac.uk/pride/archive/projects/PXD067825BloodCcells were seeded in 15-cm dishes (Greiner Cellstar) and grown to 70-80% confluence prior to induction with 1µg/ml doxycycline for 22 h. GFP-protein expression was verified using ZOE fluorescence microscopy (Biorad). Next, induced cells were harvested and nuclear and cytoplasmic extracts were obtained using a modified version of the Dignam procedure. Protein concentrations were determined by Bradford assay (BioRad). 1 mg of nuclear extract was used for GFP-affinity purification as described. In short, protein lysates were incubated in binding buffer (20 mM Hepes-KOH pH 7.9, 300 mM NaCl, 20% glycerol, 2 mM MgCl2, 0.2 mM EDTA, 0.1% NP-40, 0.5 mM DTT and 1x Roche protease inhibitor cocktail) on a rotating wheel for 1 h at 4oC in triplicates with GBP-coated agarose beads (Chromotek) or control agarose beads (Chromotek). The beads were washed two times with binding buffer containing 0.5% NP-40, two times with PBS containing 0.5% NP-40, and two times with PBS. On-bead digestion of bound proteins was performed overnight in elution buffer (100 mM Tris-HCl pH 7.5, 2 M urea, 10 mM DTT) with 0.1 µg/ml of trypsin at RT and eluted tryptic peptides were bound to C18 stagetips (ThermoFischer, USA) prior to mass spectrometry analysis. Tryptic peptides were eluted from the C18 stage tips in H2O:acetonitril (35:65) and dried prior to resuspension in 10% formic acid. A third of this elution was analyzed by nanoflow-LC-MS/MS with an Orbitrap Fusion Lumos mass spectrometer coupled to an Easy nano-LC 1200 HPLC (Thermo Fisher Scientific). The flow rate was 300 nl/min, buffer A was 0.1 % (v/v) formic acid and buffer B was 0.1 % formic acid in 80 % acetonitrile. A gradient of increasing organic proportion was used in combination with a reversed phase C18 separating column (2 µm particle size, 100 angstron pore size, 25 cm length, 50 µm i.d., Thermo Fisher Scienitific). Each MS can was followed by a maximum of 10 MS/MS scans in the data dependent mode with 90 min total analysis time. Blank samples consisting of 10% formic acid were run for 45 min between GFP and non-GFP samples, to avoid carry-over between runs.PrideNot availableThe raw data files were analyzed with MaxQuant software (version 1.5.3.30) using Uniprot human FASTA database. Label-free quantification values (LFQ) and match between run options were selected. Intensity based absolute quantification (iBAQ) algorithm was also activated for subsequent relative protein abundance estimation. The obtained protein files were analyzed by Perseus software.ProteomicsMarc TimmersGerman Cancer Consortium (DKTK), partner site Freiburg German Cancer Research Center (DKFZ) Foundation under Public Law c/o Department of Urology Zentrale Klinische Forschung (ZKF) Medical Center-University of Freiburg Breisacher Str. 66, 79106 Freiburg, GermanyPARTIALHomo Sapiens (human)42371796 Ozyerli-Goknar E, Nizamuddin S, Fetsch V, Biniossek ML, Hartmann A, Perner F, McGeehan GM, Armstrong SA, Zeiser R, Timmers HTM. Menin-MLL inhibitors enhance JUND activity in MLLr leukemic cells contributing to tumorigenesis and therapy resistance. Blood. 2026:blood.2025032363 10.1182/blood.2025032363m.timmers@dkfz-heidelberg.deGerman Cancer Consortium (DKTK), partner site Freiburg German Cancer Research Center (DKFZ) Foundation under Public Law c/o Department of Urology Zentrale Klinische Forschung (ZKF) Medical Center-University of Freiburg Breisacher Str. 66, 79106 Freiburg, GermanyGermanyMLL-rearranged (MLLr) acute myeloid leukemia (AML) and acute lymphoid leukemia (ALL) involve reciprocal translocations of the KMT2A (MLL1) gene with various translocation partner genes, which yields oncogenic chimeric MLL1 fusion proteins (MLL-FPs). Menin, the protein product of the MEN1 gene, is essential for the leukemogenic activity of MLL-FPs. Revumenib is a small-molecule inhibitor that selectively disrupts the menin-MLL interaction, and it is now in clinical use for treatment of MLLr and NPM1-mutated (NPM1c) acute leukemia. Notably, menin also interacts with the JUND member of the AP-1 transcription factor family through a conserved protein sequence in the MLL1/2 binding pocket of menin. Despite this structural similarity, the impact of menin-MLL inhibitors on JUND function has remained unexplored. Here, we investigated the influence of menin-MLL inhibitors on JUND activity. Quantitative mass spectrometry analysis of MLLr leukemic cells demonstrated that menin-MLL inhibitors also disrupt menin-JUND interactions. Furthermore, CRISPR-mediated inactivation of JUND or pharmacological inhibition using JNK inhibitors synergistically enhanced the anti-leukemic effects of menin-MLL inhibitors leading to reduced cell proliferation, cell cycle arrest and apoptosis. RNA sequencing and chromatin binding assays revealed that menin-MLL inhibitor treatment increased JUND chromatin occupancy leading to upregulation of target genes and contributing to resistance against menin-MLL inhibitors. Immunocompromised mice engrafted with JUND-deficient leukemia cells exhibited reduced tumor burden compared to control mice engrafted with wild type leukemic cells. These findings reveal a role for JUND in MLLr AML and suggest that targeting JUND transcription factor activity enhances the efficacy of menin-MLL inhibitors towards MLLr leukemic cells.Menin-MLL inhibitors enhance JUND activity in MLLr leukemic cells contributing to tumorigenesis and therapy resistance.Ozyerli-Goknar Ezgi E, Nizamuddin Sheikh S, Fetsch Viktor V, Biniossek Martin L ML, Hartmann Alina A, Perner Florian F, McGeehan Gerard M GM, Armstrong Scott A SA, Zeiser Robert R, Timmers H T Marc HTMfalseMenin-MLL inhibitors enhance AP-1 transcription factor JUND activity in MLLr leukemic cells which contributes to tumorigenesis and therapy resistance (sampleIDs - EO241-EO252; MV-411 cell lines)Background: MLL-rearranged (MLLr) acute myeloid leukemia (AML) and acute lymphoid leukemia (ALL) involve reciprocal oncogenic translocations of the KMT2A/KMT2B (MLL1/MLL2) gene on chromosome 11q23 with various translocation partner genes, which yields to chimeric MLL fusion proteins (MLL-FPs). Menin, the protein product of the MEN1 gene, is essential for the leukemogenic activity of MLL-FPs. Revumenib, a small-molecule inhibitor that selectively disrupts the menin-MLL interaction, has recently received FDA approval for clinical use for the treatment of adult and pediatric patients with relapsed or refractory MLLr acute leukemia. Notably, menin also interacts with the AP-1 transcription factor JUND through a conserved sequence identical to that required for MLL-FP binding. Despite this structural similarity, the impact of menin-MLL inhibitors on JUND function has remained unexplored. Results: In this study, we investigated the influence of menin-MLL inhibitors on JUND activity. Quantitative mass spectrometry analysis of MLLr leukemia cells treated with menin-MLL inhibitors demonstrated that they also disrupt menin-JUND protein interactions. Furthermore, CRISPR-mediated inactivation of JUND or pharmacological inhibition using JNK inhibitors synergistically enhanced the anti-leukemic effects of menin-MLL inhibitors, leading to reduced cell proliferation, cell cycle arrest and apoptosis. RNA sequencing and chromatin binding assays revealed that menin-MLL inhibitor treatment increases JUND chromatin occupancy, leading to upregulation of target gene expression and potentially contributing to the development of resistance to menin-MLL inhibitors. Mouse models engrafted with JUND-deficient leukemia cells exhibited reduced tumor burden compared to control mice engrafted with wild type leukemic cells. Conclusion: These findings suggest that targeting JUND activity may significantly enhance the efficacy of menin-MLL inhibitors towards MLLr leukemia 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