{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_29.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_16.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_09.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_21.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_32.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_28.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_24.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_17.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_20.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/20231109_E1_Neo_CollD_AUR02_25cm_SK_MS-0036_sample_25.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067742/Interactome_Search.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["wbecker@ukaachen.de"],"submitter":["Sebastian Kallabis"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Hek293","Rfx7","Dyrk1a","Dyrk1b","P53"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067742"],"tissue":["Cell Culture"],"sample_protocol":["Sample preparation for LC-MS/MS analysis FLAG-RFX7 was immunoprecipitated from transiently transfected HEK293tsa cells as described in the method section of the main paper. A total of 50 μl Urea lysis buffer (8 M urea, 10 mM Bond-Breaker TCEP solution, 30 mM CAA in 50 mM Tris-HCl buffer pH 8.5) was vadded to the pelleted anti-FLAG M2 affinity beads (#A2220, Sigma-Aldrich, St. Louis, MO, USA) and incubated at room temperature in a thermo shaker at 800 for 30 min. Following, samples were equally split, diluted with 50 mM Tris-HCl to a concentration of <2 M Urea, and digested either with trypsin/Lys-C or chymotrypsin (both 500 ng/sample, Promega) at room temperature and 800 g in a thermo shaker overnight. The next day, samples were acidified with formic acid (final concentration 0.5 %) and desalted using a modified C18 StageTip protocol. In-house-made polystyrene-divinylbenzene reversed phase sulfonate (SDB-RPS, Affinisep) double-layer StageTips were activated with 100 μl methanol and washed twice with 100 μl buffer B. The tips were equilibrated with 100 μl buffer A, and samples were loaded onto the StageTips. Bound peptides were washed once with 200 μl buffer A and twice with 200 μl buffer B. After each step, samples were centrifuged at 500 g for 1 min or until all liquid passed through the SDB-RPS material. Peptides were eluted with 60 μl buffer X (80% ACN, 5% ammonia in LC-MS-grade water) and vacuum-dried in a vacuum centrifuge. Peptides were resuspended in 10 μl buffer R, peptide concentrations were determined, and 200 ng was injected into the LCMS systems. Liquid chromatography-mass spectrometry: A liquid chromatography-tandem mass spectrometry system consisting of a Vanquish Neo UHPCL operated in trap mode, and an Orbitrap Exploris 480 MS (both Thermo Fisher Scientific) was used for proteomics analysis. Peptides were separated with a 60-minute chromatographic gradient consisting of a binary buffer system with buffer A (0.1 % formic acid in LC-MS-grade water) and buffer B (0.1 % formic acid, 80% acetonitrile in LC-MS-grade water). An IonOpticks Aurora Ultimate analytical column was used for peptide separation. The LC-MS system was operated in data-dependent acquisition (DDA) mode. Buffer B was linearly increased from 2 – 34% over 41 minutes, followed by an increase to 50% over 6 minutes. For the remaining 13 minutes, the analytical column was washed at 95% buffer B. Full MS were acquired at a resolution of 60,000, an injection time of 25 ms, and an AGC target of 300%. Per cycle, 20 potential precursor ions were selected for fragmentation from a range of 350 – 1,750 m/z with an isolation width of 1.4 m/z. Fragment spectra were acquired at a resolution of 15,000, an injection time of 22 ms and an AGC target of 100%. Peptides were fragmented by HCD operated at 27%."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw data was processed in MaxQuant using the implemented Andromeda search engine (version 2.4.3.0; Cox et al. 2008, Cox et al. 2011). Default settings were applied, except trypsin or chymotrypsin was selected as the digestion enzyme. The SWISS-PROT Homo sapiens database (downloaded 2023-02-15) was used, complemented with the Mus musculus RFX7 sequence (F8VPJ6), replacing the human RFX7 version.  The statistical analysis was performed with Perseus (v. 1.6.15, Tyanova et al. 2016). Protein LFQ intensities were log2-transformed and filtered for data completeness in at least one condition. Missing protein intensities were replaced sample-wise by random selection of values from a 1.8 standard deviations downshifted, 0.3 standard deviations broad normal distribution. Identification of significantly enriched proteins was performed by Welch's t-testing (S0 = 0.1, permutation-based FDR correction = 0.05, with 250 randomisations)."],"omics_type":["Proteomics"],"labhead":["Walter Becker"],"instrument_platform":[""],"labhead_affiliation":["Institute of Pharmacology and Toxicology, RWTH Aachen University, 52074 Aachen, Germany"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["kallabis@uni-bonn.de"],"publication":["10.1038/S41419-026-08660-X"],"submitter_affiliation":["Core Facility Translational Proteomics\nMedical Faculty\nUniversity Bonn\nVenusberg - Campus 1\n53127 Bonn Germany"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"The protein kinase DYRK1B is a p53 target gene and functions as a negative feedback regulator of the transcription factor RFX7 - Interactome","description":"The tumor suppressor protein p53 orchestrates cellular responses to stress by regulating the transcription of target genes involved in processes such as cell cycle control, DNA damage repair and apoptosis. The protein kinase DYRK1B, known to promote cancer cell survival and contribute to DNA damage repair, is overexpressed in various tumor types. Here, we demonstrate that expression of DYRK1B - but not its closely related paralog DYRK1A - is upregulated by cytostatic drugs (Actinomycin D, Doxorubicin) in multiple cancer cell lines. This induction required functional p53 and was mediated by p53-dependent activation of the transcription factor RFX7. Furthermore, we show that DYRK1B physically interacts with RFX7 and counteracts its activation by p53, thereby establishing a negative feedback loop that attenuates RFX7- dependent gene expression. This inhibitory effect of DYRK1B was strictly dependent on its catalytic activity and could be blocked by using small-molecule DYRK1 inhibitors. In conclusion, our study identifies DYRK1B as an indirect p53 target that suppresses p53- mediated activation of RFX7. These findings suggest that pharmacological inhibition of DYRK1B may represent a therapeutic strategy to enhance RFX7 tumor suppressor 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