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Half of each tumor was taken and lysed in 500uL ice-cold lysis buffer (Pierce RIPA lysis buffer, 1x HALT protease/phosphatase inhibitor, 1x Pierce universal nuclease) by homogenization in a BeatBox (PreOMICS) set to high power for 20mins. Lysates were centrifuged at 13,000rcf for 10 minutes at 4C to remove insoluble material. Protein concentrations were then determined using the Pierce Rapid Gold BCA kit. Protein lysates for proteomics were processed for mass spec analysis using an OpenTrons Flex liquid handling robot adapted to perform the Single-Pot Solid-Phase Sample Preparation (SP3) method. In quadruplicate, fifty µg of total protein of each lysate were reduced, alkylated, digested into peptides with trypsin and endopeptidase LysC. Tryptic peptides were desalted with Affinisep C18 StageTips, resuspended, separated by reversed-phase nano liquid chromatography with an IonOpticks Aurora Ultimate XT 25cm x 75um C18 UHPLC column and analyzed online with a Thermo Scientific Orbitrap Astral mass spectrometer operated in narrow window data-independent acquisition (DIA) mode."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Raw data were processed with DIA-NN version 1.8.1 and searched against a comprehensive SwissProt sequence database release (date: 15 January 2019) using the library-free setting. Downstream bioinformatics analysis was performed using the R statistical programming language. Evidence was filtered for precursors present in at least 60% of all samples with a minimum of two distinct amino acid sequences detected per protein. Protein quantification was then performed at the gene level using the MaxLFQ algorithm. An unpaired limma test was applied to compare KTX-169 and vehicle treated samples. Statistical results of proteins were only reported if a protein was quantified in at least 50% of all replicate samples in both test groups. To determine significance, a weighted significance cutoff was applied which factors in both statistical significance and fold-change."],"omics_type":["Proteomics"],"labhead":["Kirti Sharma"],"instrument_platform":[""],"labhead_affiliation":["Kymera Therapeutics, United States"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["proteomics_user@kymeratx.com"],"submitter_affiliation":["Kymera Therapeutics"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Targeted degradation of MDM2 overcomes feedback regulation of p53 signaling in Merkel cell carcinoma models.","description":"This study explores the efficacy of MDM2 degraders, KTX-049 and KT-253, in treating Merkel cell carcinoma (MCC), an aggressive skin cancer. MCC tumors often exhibit clonal integration of Merkel cell polyomavirus, with virus-positive (MCCP) and virus-negative (MCCN) tumors showing distinct molecular profiles. MDM2, a target of the ST-MYCL-Tip60 complex in MCCP, inhibits p53-mediated tumor suppression. Our results demonstrate that KTX-049 is over 100 times more potent than the MDM2 inhibitor DS-3032 in MCC cell lines with wild-type p53, effectively degrading MDM2 and activating a p53 response. Mathematical modeling suggests that KTX-049 disrupts the p53-MDM2 feedback loop, enhancing its potency. In vivo, KT-253 showed significant tumor growth inhibition in patient-derived xenograft models. However, observed resistance was linked to TP53 mutations. These findings highlight the potential of MDM2 degraders as a therapeutic strategy for MCC tumors with wild-type p53 and underscore the need for further investigation into resistance mechanisms and combination 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