{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/checksum.txt"],"Pdf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/Corresponding_Names.pdf"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_3_IMAC_F38476_201210172923.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_5_TiO2_F38484_201211194308.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_4_IP_F38589.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_1_IP_F38586.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_1_TiO2_F38480_201211063615.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_4_TiO2_F38483_201211162623.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_2_IP_F38587_201215092826.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_4_IMAC_F38477_201210204606.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_3_IP_F38588.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_6_IP_F38591.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_2_TiO2_F38481_201211095257.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_1_IMAC_F38474_201210105552.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_3_TiO2_F38482_201211130940.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_5_IP_F38590_201215105516.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_6_IMAC_F38479_201211031932.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_5_IMAC_F38478_201211000249.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_6_TiO2_F38485_201211225950.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/StMA200610_phospho_MOLM_2_IMAC_F38475_201210141240.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066447/result.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["stephane.manenti@inserm.fr"],"submitter":["Emilie-Fleur GAUTIER"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Acute Myeloid Leukemia"],"software":[""],"submitter_keywords":["Translation","Cell cycle","Rna binding proteins","Lc-ms/ms","Mrna","Cdc25a"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD066447"],"tissue":["Cell Culture","Myeloid Cell"],"sample_protocol":["Cells that grew in SILAC medium were lysed in a buffer containing 2% Sodium Deoxycholate, 10 mM TCEP, 40 mM CAA, 100 mM Tris then boiled 5 minutes at 95°C. Samples were sonicated by diagenode during 45 minutes before being boiled again 5 minutes at 95°C. MgCl2 (1 mM final) and 1 µl of benzonase were added, then samples were incubated 1h at room temperature. 4 ml of cold acetone was added and samples were placed at -20°C overnight. After cold centrifugation for 15 min at 10 000g, washing with 2 * 1ml of cold acetone, the pellet was dried and solubilized in 1 ml of TEAB 100 mM-TFE 10%. Samples were digested overnight with trypsin 1/50 and LysC 1/250. Peptides were then speed-vacuum dried and phospho-tyrosine phosphorylated peptides were immunoaffinity purified using the PTM Scan Phospho-Tyrosine Rabbit mAb, following the protocol provided by the kit (Cell signalling P-Tyr-1000 Kit #8803).  TFA was added to the unbound peptides to reach 2% final, then peptides were cleaned up at room temperature on Sep-Pak columns (C18 from Waters Corporation WAT036905). The column was equilibrated and washed successively with ACN, 50% ACN-0.1% TFA and 0.1% TFA. Once the peptides are attached, they are washed with 0.1% TFA and eluted 3 times with 80% ACN-0.5% TFA before being freeze-dried. The peptides were solubilized in 1% FA-40% ACN before being purified on IMAC beads (Phos-select Iron Affinity gel, Sigma P9740). The beads were washed 3 times in a solution containing 1% FA-40% ACN before being incubated for 1 hour at room temperature with the peptides (20 µl of beads/mg of peptides). The unbound peptides were resuspended and then placed on new washed beads and the mixture was incubated again for 1 hour. The unbound peptides were pooled and freeze-dried. The IMAC beads are deposited on a 6-layer C18 stage-tip (3M Empore Dics, 2215-C18) previously washed with ACN and a solution containing 50% ACN-0.1% TFA. They are then washed 3 times with 1% FA-40% ACN, 2 times with 1% FA. The phosphorylated peptides were eluted from the beads with 500mM KHPO4 pH7, then washed 2 times with 1% FA and then eluted from the C18 phase with 40% ACN-1% FA. The 2 incubations on beads were pooled before being dried in speed-vac. The unbound peptides following IMAC purification were solubilized in 2M lactic acid-50% ACN. They were purified on TiO2 beads (GlSciences, 5020-75000) previously washed with 2M lactic acid-50% ACN (1 mg of TiO2/mg of peptides). The bead/peptide mixture was incubated for 1 hour at room temperature. The unbound peptides were incubated on new beads for 1 hour. The TiO2 beads were deposited on a 2-layer C8 stage-tip (3M Empore Dics, 2214-C8) previously washed with methanol and a solution containing 50% ACN-0.1% TFA. They were then washed 1 time with 60% ACN-1% TFA. The phosphorylated peptides were eluted from the beads, two times, with 40% ACN- 15% NH4OH 28%, then neutralized with TFA20%. The 2 incubations on beads were pooled before being dried in speed-vac. For each purification (immunoaffinity, via IMAC beads, via TiO2 beads), phosphopeptides were separated by Reverse phase C18 using an u3000 RSLC chromatographic system from Dionex on a 2 µm particle size, 100 Angström pore size, 75 µm internal diameter, 25 cm length C18 reverse phase analytical column with a 150 min binary gradient from 99% solution A (0.1% FA in H2O) to 55% solution B (80% ACN, 0.085% FA) before injection into an Orbitrap Fusion Mass Spectrometer MS (from Thermo Scientific). MS data acquisition was performed throughout the elution process in a data-dependent scheme (top speed mode in 5 seconds) with full MS scans acquired with the orbitrap detector, followed by HCD peptide fragmentation and Ion trap fragment detection of the most abundant ions detected in the MS scan. Mass spectrometer settings for full scan MS were: 2.0E5 AGC, 60,000 target resolution, 350-1500 m/z range, maximum ion injection time (MIIT) of 60 ms. HCD MS/MS fragmentation was permitted for 2-7+ precursor ions reaching more than 5.0E3 minimum intensity. Quadrupole-filtered precursors within 1.6 m/z isolation window were fragmented with a Normalised Collision Energy setting at 30. 2.0E4 AGC Target and 100 ms MIIT were the limiting ions accumulation values. The Ion-trap detector was used for its fast and sensitive detection capabilities. A 30 seconds dynamic exclusion time was set."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Maxquant software version 1.6.17.0 (Cox. J et al. 2014) was used for the data extraction from the raw MS files from mass spectrometer. For each sample, the data from each purification were pooled. The databases used were the human sequences from the Uniprot database (March 2020, 42384 entries) and a list of in-house frequent contaminant sequences. The cleavage specificity was trypsin’s with maximum 2 missed cleavages. Carbamidomethylation of cysteines was set as constant modification, whereas acetylation of the protein N terminus, oxidation of methionines and phosphorylation of serine, threonine and tyrosine were set as variable modifications. The false discovery rate was kept below 1% on both peptides and proteins. The “match between runs” (MBR) option was allowed with a match time window of 1 min and an alignment time window of 30 min. For statistical analysis, data were imported into the Perseus software version 1.6.14.0 (Tyanova. S et al 2016). Reverse and contaminant proteins were excluded from analysis."],"omics_type":["Proteomics"],"labhead":["Stéphane Manenti"],"instrument_platform":[""],"labhead_affiliation":["University of Toulouse, INSERM, CNRS, CRCT, France"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["ef.gautier.upd@gmail.com"],"publication":["42448957 Shin S,Cargnello M,Pinchedé L,Medale Giamarchi C,Villette C,Gay A,Salnot V,Gautier EF,Dassi E,Millevoi S,Cammas A,Manenti S Novel CDK-independent function of CDC25 phosphatases in mRNA translation. EMBO Rep. 2026 Jul 14 10.1038/s44319-026-00852-y"],"submitter_affiliation":["Proteom’IC facility, Université Paris Cité, CNRS, INSERM, Institut Cochin, F-75014 PARIS, France"],"submitter_country":["France"],"pubmed_abstract":["Molecular and functional networks driving coordination between cell cycle and mRNA translation remain to be explored. Here, we use mass spectrometry-based proteomics to comprehensively investigate the interactome and phosphoproteome of the cell cycle regulator CDC25A. We identify actors of mRNA regulation, such as RNA-binding proteins and translation factors, as interacting partners of CDC25A. CDC25A overexpression increases global translation, whereas catalytic inactivation or pharmacological inhibition decreases protein synthesis. A Cyclin-Dependent Kinase (CDK) interaction-deficient mutant of CDC25A also enhances translation, indicating a CDK-independent role. Our results further reveal an interplay between CDC25A and CDC25B whereby downregulation of CDC25A leads to compensatory overexpression of CDC25B. The roles of CDC25A and CDC25B in mRNA translation are independent of their roles in the cell cycle, with CDC25A possibly regulating translation elongation and CDC25B rather involved in initiation. In acute myeloid leukemia cells, CDC25A depletion also inhibits translation, suggesting its potential relevance as a therapeutic target. We propose that CDC25 phosphatases might be signaling platforms coordinating cell cycle progression with protein synthesis."],"pubmed_title":["Novel CDK-independent function of CDC25 phosphatases in mRNA translation."],"pubmed_authors":["Shin Sauyeun S, Cargnello Marie M, Pinchedé Lisa L, Medale Giamarchi Claire C, Villette Cléa C, Gay Alexandre A, Salnot Virginie V, Gautier Emilie-Fleur EF, Dassi Erik E, Millevoi Stefania S, Cammas Anne A, Manenti Stéphane S"],"additional_accession":[]},"is_claimable":false,"name":"Phosphoproteomic analysis of leukemic cells after RNA interference-mediated depletion of CDC25A","description":"Molecular and functional networks driving coordination between cell cycle and mRNA translation remain to be explored. Here, we used mass spectrometry-based proteomics to comprehensively investigate the interactome and phosphoproteome of the cell cycle regulator CDC25A. This highlighted several actors of mRNA regulation, such as RNA-binding proteins and translation factors, as interacting partners of CDC25A. Ectopic overexpression of CDC25A increased global translation without affecting the cell cycle, while inhibiting CDC25 phosphatases rapidly decreased protein synthesis. A Cyclin Dependent Kinase (CDK) interaction-deficient mutant of CDC25A also enhanced translation, indicating a CDK-independent role. Our results revealed an interplay between CDC25A and CDC25B whereby down-regulation of CDC25A led to compensatory overexpression of CDC25B, while down-regulation of CDC25B was not compensated by CDC25A, reducing mRNA translation. Notably, the roles of CDC25A and CDC25B in mRNA translation are independent of the cell cycle, with CDC25A regulating elongation and CDC25B rather involved into initiation. Finally, we confirmed the implication of CDC25A in translation in acute myeloid leukemia cell lines, in which RNA interference-mediated depletion of CDC25A inhibited translation. Altogether, we propose that CDC25 phosphatases can be considered as signaling platforms coordinating cell cycle progression with mRNA translation and protein synthesis.","dates":{"publication":"2026-07-15","submission":"2025-07-23"},"accession":"PXD066447","cross_references":{"TAXONOMY":["NEWT:68239","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:37919","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:460523","NEWT:2423","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:291146","NEWT:29466","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:941638","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:9938","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:483179","NEWT:315750","NEWT:99490","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:1479235","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4233","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:2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