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The cells were treated with either KI-CDK9d-32 or DMSO. A total of four biological replicates were prepared. Samples specified as below:   Condition Treatment Time_point Bio_replicate TMT_Channel DMSO_4_3 Vehicle 4 3 TotInt_126C_rs221117_MT_plex_Phospho_action DMSO_4_4 Vehicle 4 4 TotInt_127N_rs221117_MT_plex_Phospho_action D32_4_1 KI-CDK9d-32 4 1 TotInt_127C_rs221117_MT_plex_Phospho_action D32_4_3 KI-CDK9d-32 4 3 TotInt_128N_rs221117_MT_plex_Phospho_action DMSO_1_3 Vehicle 1 3 TotInt_128C_rs221117_MT_plex_Phospho_action D32_1_3 KI-CDK9d-32 1 3 TotInt_129N_rs221117_MT_plex_Phospho_action D32_1_1 KI-CDK9d-32 1 1 TotInt_129C_rs221117_MT_plex_Phospho_action D32_4_2 KI-CDK9d-32 4 2 TotInt_130N_rs221117_MT_plex_Phospho_action DMSO_4_1 Vehicle 4 1 TotInt_130C_rs221117_MT_plex_Phospho_action DMSO_1_2 Vehicle 1 2 TotInt_131N_rs221117_MT_plex_Phospho_action DMSO_1_1 Vehicle 1 1 TotInt_131C_rs221117_MT_plex_Phospho_action DMSO_1_4 Vehicle 1 4 TotInt_132N_rs221117_MT_plex_Phospho_action D32_1_4 KI-CDK9d-32 1 4 TotInt_132C_rs221117_MT_plex_Phospho_action D32_1_2 KI-CDK9d-32 1 2 TotInt_133N_rs221117_MT_plex_Phospho_action DMSO_4_2 Vehicle 4 2 TotInt_133C_rs221117_MT_plex_Phospho_action D32_4_4 KI-CDK9d-32 4 4 TotInt_134N_rs221117_MT_plex_Phospho_action  Reduction, Alkylation, and Tryptic Digestion Proteins were first reduced with 10 mM dithiothreitol (Sigma) for 1 hour at 56°C and then alkylated with 55 mM iodoacetamide (Sigma) for 1 hour at 25°C in the dark. The samples were diluted with 100 mM ammonium bicarbonate to decrease urea concentration to 1M. Proteins were digested overnight at 25°C with modified trypsin (Promega) using an enzyme-to-substrate ratio of 1:50 in 100 mM ammonium bicarbonate, pH 8.9. The reaction was stopped by adding formic acid (99.9%, Sigma) to achieve a final concentration of 5%. Samples were then desalted using Pierce Peptide Desalting Spin Columns (cat. # 89852).  TMT Labeling Desalted samples underwent TMT labeling according to Thermo Fisher Scientific’s protocol. Samples were resuspended in 100 mM TEAB, vortexed, and briefly centrifuged. Anhydrous acetonitrile (20 µL) was added to the TMT label reagents, followed by vortexing, brief centrifugation, and a 5-minute dissolution period. Then, 20 µL of TMT reagents were added to each of the 100 µL samples, which were then vortexed and briefly centrifuged. The samples were incubated for 1 hour at room temperature. To quench the reaction, 5 µL of 5% hydroxylamine was added to each sample and incubated for 15 minutes. Equal volumes of each channel were combined and concentrated to dryness via speed-vac.  Phosphopeptide enrichment A 10% aliquot of the combined TMT-labeled sample was reserved for HPLC fractionation to obtain the unmodified protein data. The remainder underwent phosphopeptide enrichment using the High-Select Fe-NTA Phosphopeptide Enrichment Kit (Thermo Fisher Scientific) as per the manufacturer's instructions.  Fractionation HPLC fractionation of non-phosphopeptides To acquire the unmodified protein data, 10% of the sample was fractionated using HPLC. The dried TMT-labeled peptides were resuspended in 10 mM TEAB and fractionated using an Agilent 1100 HPLC system with high pH buffers. Buffer A consisted of 10 mM triethylammonium bicarbonate (TEAB), and Buffer B was 10 mM TEAB in 99% acetonitrile. Fractions were collected every minute from the 10th to the 90th minute, resulting in 80 fractions. Every 15th fraction was pooled resulting in 15 total fractions for further analysis. Specifically, the 15 fractions were dried, resuspended in 10 µL of 0.2% formic acid, and 10% of this mixture was injected into the LC-MS.  High pH fractionation of Phosphopeptides Phosphopeptides were fractionated by Pierce High pH Reversed-Phase Peptide Fractionation Kit (Cat# 84868) per manufacturer’s instructions.  Dried fractions were re-suspended in 3 L of 0.2% formic acid, and 33% of this solution was injected into the LC-MS.  Liquid chromatography with tandem mass spectrometry measurement The fractionated TMT-labeled tryptic peptides were separated by reverse-phase HPLC using a Thermo Fisher Scientific PepMap RSLC C18 column before nano-electrospray ionization in an Orbitrap Exploris 480 mass spectrometer (Thermo Fisher Scientific)."],"repository":["Pride"],"labhead":["Angela N. Koehler"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Massachusetts Institute of Technology"],"publication":["40154489 Toure MA, Motoyama K, Xiang Y, Urgiles J, Kabinger F, Koglin AS, Iyer RS, Gagnon K, Kumar A, Ojeda S, Harrison DA, Rees MG, Roth JA, Ott CJ, Schiavoni R, Whittaker CA, Levine SS, White FM, Calo E, Richters A, Koehler AN. Targeted degradation of CDK9 potently disrupts the MYC-regulated network. Cell Chem Biol. 2025 32(4):542-555.e10 10.1016/j.chembiol.2025.03.001"],"submitter_affiliation":["MIT"],"labhead_mail":["koehler@mit.edu"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Acute T Cell Leukemia"],"submitter_keywords":["Cdk9","Ribosome biogenesis","Transcription","Myc","Protacs"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD052300"],"quantification_method":[""],"modification":[""],"data_protocol":["Protein identification and data pre-processing  Global quantitative mass spectrometry (Non-phosphopeptides) The raw mass spectrometry data (.raw files) were analyzed using Sequest HT within Proteome Discoverer (Thermo Fisher Scientific). The search parameters included a 10 ppm mass tolerance for precursor ions and a 0.05 Da tolerance for fragment ion mass. Up to two missed cleavages by trypsin were allowed. Fixed modifications included carbamidomethylation of cysteine and TMT labeling of lysines and peptide N-termini. Variable modifications included oxidation of methionine, phosphorylation of serine, threonine, and tyrosine, loss of methionine at the protein N-terminus, acetylation of the protein N-terminus, and combined Met-loss plus acetylation at the N-terminus. Searches were conducted against both a human protein database (homo sapiens UniProt FASTA files) and an in-house contaminant database. Peptide spectrum matches (PSMs) were exported from Proteome Discoverer (PD) and subjected to addition filtering and processing using a proteomic analysis workflow (PAW) described previously. In summary, the PD exported PSMs were filtered based on the following default pipeline criteria: a q-value cutoff of 0.05, a mass deviation within ±20 ppm, and precursor isolation interference below 50%. PSMs were further filtered by charge state (2 to 4), peptide length (6 to 28 amino acids), and rank (considering only top-ranked hits). This filtered PSMs file was then used for high confident peptide and protein inference. At least 2 distinct peptides had to be present support a protein identification within a sample, and the minimum number of tryptic termini was 2, ensuring that peptides are fully tryptic.  In a final processing step, proteins with insufficient evidence to be considered unique were grouped. Intensities are then added to the peptide and protein-level summaries and exported to R for quantitation and analysis.  Phosphopeptide Phosphopeptide raw data were processed with Proteome Discoverer version 3.0 (Thermo Fisher Scientific), peptide and protein identification were performed with Mascot version 2.4 (Matrix Science), and phosphorylation site localization probabilities were assessed using ptmRS62 within Proteome Discoverer. Spectra were searched against the UniProt homo sapiens database. Search parameters were set to trypsin digestion with a maximum of two missed cleavages. Mass tolerance was set to 10 ppm at the MS1 level and 20 mmu at the MS2 level. Precursor ions and TMT reporter ions were removed from MS/MS spectra prior to searching using the non-fragment filter node in Proteome Discoverer. Cysteine carbamidomethylation, TMT-labeled lysine, and TMT-labeled peptide N-termini were set as static modifications; phosphorylation of tyrosine, serine, and threonine, and oxidation of methionine were set as dynamic modifications.  PSMs were exported from Proteome Discoverer and filtered to keep those with high quality:  search engine rank of 1, delta mass within -10 to 10 ppm, expectation value <0.05, and ions score >15. PSMs missing values in more than 25% of TMT channels were discarded, remaining missing values were imputed with the minimum intensity observed in the dataset. Only peptides with an average abundance of 1000 or more across TMT channels, and with a ptmRS probability greater than 50 for at least one site were maintained. TMT reporter ion intensities were summed across PSMs sharing a common phosphopeptide sequence. To address the issue of redundancy, phosphopeptides derived from identical proteins with matching phosphorylation patterns were aggregated to streamline the dataset, ensuring each unique phosphosite was represented without unnecessary repetition. This aggregation was carried out by matching peptides based on their annotated sequences, modifications in master proteins, and positions in master proteins. Furthermore, motif analysis, leveraging the PhosphoSitePlus database, was carried out to map phosphorylation sites to specific known motifs."],"omics_type":["Proteomics"],"species":["Homo Sapiens (human)"],"submitter_mail":["mtoure@mit.edu"],"submitter_country":["United States"],"doi":["10.6019/PXD052300"],"pubmed_abstract":["CDK9 coordinates signaling events that regulate transcription and is implicated in oncogenic pathways, making it an actionable target for drug development. While numerous CDK9 inhibitors have been developed, success in the clinic has been limited. Targeted degradation offers a promising alternative. A comprehensive evaluation of degradation versus inhibition is needed to assess when degradation might offer superior therapeutic outcomes. We report a selective and potent CDK9 degrader with rapid kinetics, comparing its downstream effects to those of a conventional inhibitor. We validated that CDK9 inhibition triggers a compensatory feedback mechanism that dampens its anticipated effect on MYC expression and found that this was absent when degraded. Importantly, degradation is more effective at disrupting MYC transcriptional regulation and subsequently destabilizing nucleolar homeostasis, likely by abrogation of both enzymatic and scaffolding functions of CDK9. These findings suggest that CDK9 degradation offers a more robust strategy to overcome limitations associated with its inhibition."],"pubmed_title":["Targeted degradation of CDK9 potently disrupts the MYC-regulated network."],"pubmed_authors":["Toure Mohammed A MA, Motoyama Keisuke K, Xiang Yichen Y, Urgiles Julie J, Kabinger Florian F, Koglin Ann-Sophie AS, Iyer Ramya S RS, Gagnon Kaitlyn K, Kumar Amruth A, Ojeda Samuel S, Harrison Drew A DA, Rees Matthew G MG, Roth Jennifer A JA, Ott Christopher J CJ, Schiavoni Richard R, Whittaker Charles A CA, Levine Stuart S SS, White Forest M FM, Calo Eliezer E, Richters Andre A, Koehler Angela N AN"],"additional_accession":[]},"is_claimable":false,"name":"Targeted Degradation of CDK9 Potently Disrupts the MYC Transcriptional Network","description":"Cyclin-dependent kinase 9 (CDK9) coordinates signaling events that regulate RNA polymerase II (Pol II) pause-release states. It is an important co-factor for transcription factors, such as MYC, that drive aberrant cell proliferation when their expression is deregulated. CDK9 modulation offers an approach for attenuating dysregulation in such transcriptional programs. As a result, numerous drug development campaigns to inhibit CDK9 kinase activity have been pursued. More recently, targeted degradation has emerged as an attractive approach. However, comprehensive evaluation of degradation versus inhibition is still critically needed to assess the biological contexts in which degradation might offer superior therapeutic benefits. We validated that CDK9 inhibition triggers a compensatory mechanism that dampens its effect on MYC expression and found that this feedback mechanism was absent when the kinase is degraded. Importantly, CDK9 degradation is more effective than its inhibition for disrupting MYC transcriptional regulatory circuitry likely through the abrogation of both enzymatic and scaffolding functions of CDK9.","dates":{"publication":"2026-04-27","submission":"2024-05-16"},"accession":"PXD052300","cross_references":{"TAXONOMY":["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:44270","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:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:11308","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:1410384","NEWT:1310173","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:135666","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:1423687","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","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:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:476","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: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: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:11294","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:487521","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","N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