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Kirchner"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"disease":["Lymphoma"],"software":[""],"submitter_keywords":["Human","Antigen presentation","Sumo","Immunopeptidome","Mhc-i","Phosphoproteome","Cancer immunotherapy"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD060641"],"tissue":["B Cell","Blood"],"sample_protocol":["Cell pellets were resuspended in lysis buffer (1% Sodium deoxcholate, 100mM Tris-HCl pH 8, 150mM NaCl, 1mM EDTA, 40mM CAA, 10mM DTT, phosphatase inhibitor cocktail 2 and 3 (Sigma)), heated for 10 minutes at 95°C, cooled down and treated with Benzonase® (Merck, 50 units) for 30 min at 37°C. Endopeptidase LysC (Wako) and sequence-grade trypsin (Promega) were added to 100 µg protein extract (enzyme-to-protein ratio of 1:50), followed by an incubation over night at 37°C. Peptides were desalted, resuspended in 50 mM HEPES and labeled with 16-plex tandem mass tag reagents (TMTpro, Fisher Scientific) following the vendors instructions. Samples were combined, desalted, fractionated by high-pH reversed phase off-line chromatography (1290 Infinity, Agilent) and pooled into 30 fractions. 10% of each fraction was used directly for global proteome measurements. The remaining 90% were further pooled onto 15 fractions and applied to IMAC based phosphopeptide enrichment using Fe(III)-IMAC cartridges and the AssayMAP Bravo Platform (Agilent Technologies). For LC-MS/MS measurements, peptides were reconstituted in 3% acetonitrile with 0.1% formic acid and separated on a reversed-phase column (20 cm fritless silica microcolumns (inner diameter of 75 µm, packed with ReproSil-Pur C18-AQ 1.9 µm resin (Dr. Maisch GmbH)), using a 98-min gradient of increasing Buffer B (90% ACN, 0.1% FA) concentration (from 2% to 60%) with a 250 nl/min flow rate on a High-Performance Liquid Chromatography (HPLC) system (Thermo Fisher Scientific) and analyzed on an Q Exactive HF-X instrument (Thermo Fisher Scientific). The mass spectrometer was operated in data-dependent acquisition mode using 60K resolution, 350–1500 m/z scan range, maximum injection time of 10 ms. The top 20 MS/MS scan were obtained at 45K resolution with 0.7 m/z isolation window and a maximum injection time of 86 ms. Dynamic exclusion was set to 30 s and only precursor with a charge state between 2-6 were selected for fragmentation. For phosphopeptide enriched samples the maximum injection time was increased to 120 ms."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["RAW data were analyzed with MaxQuant software package (v 1.6.10.43) using the Uniprot human databases (UP000005640_2022_03). The search included variable modifications of methionine oxidation and N-terminal acetylation, deamidation (N and Q) phosphorylation (STY) and fixed modification of carbamidomethyl cysteine. Reporter ion MS2 for TMT16 was selected (internal and N-terminal) and TMT batch specific corrections factors were specified. The FDR (false discovery rate) was set to 1% for peptide and protein identifications."],"omics_type":["Proteomics"],"labhead":["Philipp Mertins"],"instrument_platform":[""],"labhead_affiliation":["Core Unit Proteomics, Berlin Institute of Health at Charité-Universitätsmedizin Berlin and Max-Delbrück-Center for Molecular Medicine, 13125 Berlin, Germany"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["41566667 Demel UM, Meurer A, Zaghla BKQ, Atay B, Steiert D, Hummel LV, Isaakidis K, Zang C, Korenkov M, Schielin M, Yousefian S, Mecklenbräuker S, Kirchner M, Haas S, Busse A, Mertins P, Müller S, Wirth M, Klatt MG, Keller U. Aberrant SUMOylation Restricts the Targetable Cancer Immunopeptidome. Adv Sci (Weinh). 2026 13(17):e11449 10.1002/advs.202511449"],"submitter_mail":["marieluise.kirchner@mdc-berlin.de"],"submitter_affiliation":["Proteomics Platform, BIH@Charite"],"submitter_country":["Germany"],"pubmed_abstract":["A balanced SUMOylation equilibrium safeguards the functional anti-tumor immune response. Oncogene activation drives SUMOylation, rendering aberrant SUMOylation a hallmark of cancer. To delineate the impact of activated SUMOylation on the tumor-immune synapse, we applied HLA class-I-targeted ligandomics and identified a function of activated SUMOylation in restricting the immunopeptidome landscape. Importantly, aberrant SUMOylation suppressed a unique HLA-I peptide and oncoprotein-derived neoepitope repertoire, enabling cancer cells to evade T cell immune surveillance. Mechanistically, SUMOylation impaired the immunoproteasome constitution and proteolytic activity, thus limiting the diversity of the peptide landscape. Further, SUMOylation altered TAP1 transporter binding preferences, thereby mimicking viral immune evasion strategies. As an actionable application, pharmacological inhibition of SUMOylation unmasked the targetable immunopeptidome, enhanced the tumor cell susceptibility to T cell killing and substantially reshaped the immune cell landscape. These findings highlight SUMOylation as a critical regulator of the adaptive anti-tumor immune response. We propose SUMOylation inhibition as a strategy to enhance immunogenic peptide presentation, thereby improving the efficacy of cancer immunotherapies."],"pubmed_title":["Aberrant SUMOylation Restricts the Targetable Cancer Immunopeptidome."],"pubmed_authors":["Demel Uta M UM, Meurer Anna A, Zaghla Badeel Kh Q BKQ, Atay Bilge B, Steiert Daniel D, Hummel Luca V LV, Isaakidis Konstandina K, Zang Chuanbing C, Korenkov Michael M, Schielin Marlon M, Yousefian Schayan S, Mecklenbräuker Shima S, Kirchner Marieluise M, Haas Simon S, Busse Antonia A, Mertins Philipp P, Müller Stefan S, Wirth Matthias M, Klatt Martin G MG, Keller Ulrich U"],"additional_accession":[]},"is_claimable":false,"name":"An oncogenic SUMO program restricts the targetable cancer immunopeptidome","description":"A balanced SUMOylation equilibrium safeguards the functional anti-tumor immune response. Oncogene activation drives SUMOylation, rendering aberrant SUMOylation a hallmark of cancer. To delineate the impact of activated SUMOylation on the tumor-immune synapse, we applied HLA class-I-targeted ligandomics and identified a function of activated SUMOylation in restricting the immunopeptidome landscape. Importantly, aberrant SUMOylation suppressed a unique HLA-I peptide and oncoprotein-derived neoepitope repertoire, enabling cancer cells to evade T cell immune surveillance. Mechanistically, SUMOylation impaired the immunoproteasome constitution and proteolytic activity, thus limiting the diversity of the peptide landscape. Additionally, SUMOylation altered TAP1 transporter binding preferences, thereby mimicking viral immune evasion strategies. As an actionable application, pharmacological inhibition of SUMOylation unmasked the targetable immunopeptidome and enhanced the tumor cell susceptibility to T cell killing. These findings highlight SUMOylation as a critical regulator of the adaptive antitumor immune response. We propose SUMO inhibition as a rational strategy to enhance immunogenic peptide presentation for more effective cancer immunotherapies.","dates":{"publication":"2026-04-06","submission":"2025-02-10"},"accession":"PXD060641","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:3715","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:717989","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:51350","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:253237","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:13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