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Savidor"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Temuterkib (ly3214996)","Bvd523 (ulixertinib)","Mek","P38","Phosphoproteomics","Gcd0994 (ravoxertinib)","Map kinase","Asn007","Cis-platin","Sch772984","Erk"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069633"],"tissue":["Spleen","Liver","Cell Culture","Muscle","Kidney"],"sample_protocol":["Cell pellets were lysed with 5% SDS in 50 mM Tris-HCl. Lysates were incubated at 96 °C for 5 min, followed by six cycles of 30 s of sonication (Bioruptor Pico, Diagenode, USA). Protein concentration was measured using the BCA assay (Thermo Scientific, USA) and a total of 120 μg protein was reduced with 5 mM dithiothreitol and alkylated with 10 mM iodoacetamide in the dark. Phosphoric acid was added to the lysates to a final concentration of 1.2%. 90:10% methanol/50 mM ammonium bicarbonate and then added to the samples. Each sample was then loaded onto S-Trap microcolumns (Protifi, USA). Samples were then digested with trypsin (1:50 trypsin/protein) for 1.5 h at 47 °C. The digested peptides were eluted using 50 mM ammonium bicarbonate; trypsin was added to this fraction and incubated overnight at 37 °C. Two more elutions were made using 0.2% formic acid and 0.2% formic acid in 50% acetonitrile. The three elutions were pooled together. An aliquot corresponding to 20 μg protein digest from each sample was set aside for total proteome analysis, while the remaining volume was used for phosphopeptide enrichment. Samples were vacuum-centrifuged to dryness and kept at −80 °C until analysis.  Phosphopeptide enrichment Phosphopeptides were enriched from the total protein digest using a ProPac IMAC-10 column (4x50mm ) (Thermo Scientific, P.N. 063276). Loading buffer (A)-0.1% TFA, 30% ACN. Elution buffer(B)- 0.3% NH4OH, pH 11.7.  Peptides were loaded on the column in 10min with flow 0.1ml/min (0% B). Phosphopeptides were eluted from the column using the following gradient: first elution from 10 to 15 min with flow 0.6ml/min (B from 0% to 15%), second elution from 15min to 44 min with flow 0.02 ml/min(B from 15% to 30%), washing from 44 min to 50 min with flow 1ml/min (B from 30% to 50%) and following equilibration from 50min to 60min with flow 1 ml/min (0%B). The phosphopeptides containing peak (second elution fraction) was collected in 1.5 ml reaction vessels (~1,2ml), vacuum-centrifuged to dryness, and reconstituted in 25 µL in 97:3 acetonitrile:water+0.1% formic acid.   Liquid chromatography  ULC/MS grade solvents were used for all chromatographic steps. Dry peptides were reconstituted in 25 µL in 97:3 acetonitrile:water+0.1% formic acid. Each sample was loaded using split-less nano-Ultra Performance Liquid Chromatography (10 kpsi nanoAcquity; Waters, Milford, MA, USA). The mobile phase was: A) H2O + 0.1% formic acid and B) acetonitrile + 0.1% formic acid. Desalting of the samples was performed online using a reversed-phase Symmetry C18 trapping column (180 µm internal diameter, 20 mm length, 5 µm particle size; Waters). The peptides were then separated using a T3 HSS nano-column (75 µm internal diameter, 250 mm length, 1.8 µm particle size; Waters) at 0.35 µL/min. For global proteomics, peptides were eluted from the column into the mass spectrometer using the following gradient: 4% to 27%B in 165 min, 27% to 90%B in 5 min, maintained at 90% for 5 min and then back to initial conditions.  For total phosphoproteomics, peptides were eluted from the column into the mass spectrometer using the following gradient: 4% to 22%B in 165 min, 22% to 90%B in 5 min, maintained at 90% for 5 min and then back to initial conditions.  Mass Spectrometry The nanoUPLC was coupled online through a nanoESI emitter (10 μm tip; New Objective; Woburn, MA, USA) to a quadrupole orbitrap mass spectrometer (Q Exactive HFX, Thermo Scientific) using a FlexIon nanospray apparatus (Proxeon).  Data was acquired in data dependent acquisition (DDA) mode, using a Top10 method. For global proteomics MS1 resolution was set to 120,000 (at 200m/z), mass range of 375-1650m/z, AGC of 3e6 and maximum injection time was set to 60msec. MS2 resolution was set to 15,000, quadrupole isolation 1.7m/z, AGC of 1e5, dynamic exclusion of 45sec  and maximum injection time of 60msec. For phosphoproteomics similar parameters were used with the exception of MS2 maximum injection time of 150msec."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw data was processed with MaxQuant v1.6.6.0. The data was searched with the Andromeda search engine against the mouse (Mus musculus) protein databases as downloaded from Uniprot (www.uniprot.com), appended with common lab protein contaminants and the recombinant human WT or mutant ERK1 sequences. Enzyme specificity was set to trypsin and up to two missed cleavages were allowed. Fixed modification was set to carbamidomethylation of cysteines. For global proteomics variable modifications were set to oxidation of methionines, asparagine and glutamine deamidation, and protein N-terminal acetylation. For phosphoproteomics, phosphorylation of S, T, or Y were additionally included as variable modifications. Peptide precursor ions were searched with a maximum mass deviation of 4.5 ppm and fragment ions with a maximum mass deviation of 20 ppm. Peptide and protein identifications were filtered at an FDR of 1% using the decoy database strategy (MaxQuant’s “Revert” module). The minimal peptide length was 7 amino-acids and the minimum Andromeda score for modified peptides was 40. Peptide identifications were propagated across samples using the match-between-runs option checked. Searches were performed with the label-free quantification option selected. The quantitative comparisons were calculated using Perseus v1.6.0.7. Decoy hits were filtered out and only proteins that were detected in at least two replicates of at least one experimental group were kept. Empty intensity values went through imputation using the corresponding Perseus function. A Student’s t-Test, after logarithmic transformation, was used to identify significant differences between the experimental groups, across the biological replica. Fold changes were calculated based on the ratio of geometric means of the different experimental groups."],"omics_type":["Proteomics"],"labhead":["Prof. David Engelberg"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Dept. of Biological Chemistry The Institute of Life Science The Hebrew University of Jerusalem Jerusalem 91904, Israel"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["alon.savidor@weizmann.ac.il"],"submitter_affiliation":["The Weizmann Institute of Science"],"submitter_country":["Israel"],"additional_accession":[]},"is_claimable":false,"name":"Similar effects of various Erk inhibitors: interception of negative feedback, activation of p38, imposing cell cycle arrest, and maintaining cell viability","description":"The MAP kinases Erk1/2 are the major mediators of the oncogenicity of the Receptor tyrosine kinase (RTK)-Ras-Raf-MEK cascade. As components of this pathway are often mutated and constantly active in cancer, Erks are regarded as promising targets for therapy for many types of malignancies. Yet, while active Erks are promoting abnormal cell proliferation, they simultaneously also inhibit upstream components of the pathway. Erks’ inhibition causes, therefore, reactivation of proto-oncogenic proteins hence Erks’ inhibitors must be applied causiously. Here we studied the effects of Erks’ inhibitors on cells transformed by oncogenic variants of Erk1, Erk1R84H and Erk1R84S, in which the negative feedback effect is so powerful that Erks’ phosphorylation could not be monitored. We show that provision of either BVD523, SCH772984, ASN007, Temuterkib or GCD0994, led to re-appearance of high phosphorylation levels of Erks, suggesting that all inhibitors intercepted Erks-mediated negative feedback activity. We found that inhibitors-mediated Erks’ re-phosphorylation is dependent entirely on MEK activation and that the highly phosphorylated Erk molecules are catalytically inactive. All inhibitors caused cell cycle arrest at the G1 phase, by inducing elevation of p21Cip1/Waf1 and Klf4, but did not affect cell viability for at least 72 hours. They also caused activation of the MAP/stress kinase p38. Proteome and phosphoproteome analysis of BVD523-treated cells revealed effect of the drug on the Rho GTPase pathway and on MAPK targets. The 5 inhibitors were further tested on a battery of 9 cancer-derived cell lines and in many of them most of the effects were similar to those observed with the Erk1R84H- and Erk1R84S-transformed NIH3T3 cells","dates":{"publication":"2026-05-18","submission":"2025-10-19"},"accession":"PXD069633","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:510516","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:441772","NEWT:48106","NEWT:295027","NCBI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