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Reber"],"technology_type":["Data-dependent acquisition","Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Bioid","Structural proteomics","Ap-ms","Lip-ms","Proximity labeling"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069830"],"tissue":["Early Embryonic Cell"],"sample_protocol":["Cultivation of cells  HEK293 cells inducibly expressing the tagged bait proteins were seeded at 10^6/ml in 25 ml DMEM supplemented with 10% FBS and 1% P/S in a 15 cm dish. Protein expression was induced with 1.3 μg/ml doxycycline for 24 hours. AP-MS and proximity labeling samples were treated with 1 μM inhibitor in 0.01% DMSO for 4 hours. For proximity labeling samples, cells were treated with 50 μM biotin an hour before harvesting. AP-LiP-MS Pellets were lysed in 2 ml HNN buffer (50 mM HEPES pH = 8, 150 mM NaCl, 50 mM NaF) supplemented with 0.5% IGEPAL, 400 nM sodium orthovanedate, 1 mM PMSF and 0.2% Protease Inhibitor Cocktail. The lysate was incubated on ice for 10 minutes and centrifuged at 18000x g for 20 minutes at 4 °C. The supernatant was added to 80 μl StrepTatcin Sepharose resin and incubated on a rotating wheel for 60 minutes at 4 °C. The beads were loaded onto a 1 μm glass filter column and washed 3 times with 1 ml HNN buffer supplemented with 0.5% IGEPAL and 400 nM Na3VO4, 3 times with 1 ml HNN buffer, and 3 times with LiP buffer (1 mM MgCl2, 150 mM KCl and 100 mM HEPES pH 7.5). Samples were eluted twice by incubation with 30 μl of 0.5 mM biotin in LiP buffer for 15 minutes. The eluate was pooled and the total protein concentration was determined using a BCA protein assay kit according to manufacturer’s protocol. Samples were treated with 10 μM inhibitor or 2% DMSO in triplicates and incubated at 25˚C for 5 minutes. Proteinase K at an enzyme:substrate ratio of 1:100 was added for 5 minutes. Proteolysis was stopped by incubation at 99 °C for 5 minutes. Samples were then diluted with 10% sodium deoxycholate (DOC) for a final concentration of 5% DOC.  AP-MS Pellets were lysed as for AP-LiP-MS samples except those using PRKCA as bait, in which 1% DDM was used instead, 400 nM Na3VO4, 1 mM PMSF and 0.2% Protease Inhibitor Cocktail. The pulldown was done as for AP-LiP-MS samples, except that the final wash was done with 100 mM ammonium bicarbonate. Samples were eluted twice by incubation with 30 μl of 0.5 mM biotin in 100 mM ammonium bicarbonate for 15 minutes. To the samples, 60 μl 8 M urea in 100 mM ammonium bicarbonate was added for a final concentration of 4 M urea. Proximity labeling Samples were lysed in 1 ml RIPA buffer (50 mM Tris-HCl pH 8, 150 mM NaCl, 1 % Triton, 1mM EDTA, 0.1 % SDS) supplemented with 1 mM PMSF and 0.2% Protease Inhibitor Cocktail. The lysate was briefly sonicated for 30 s, incubated at 10 °C for 30 minutes and centrifuged at 18000x g for 20 minutes at 4 °C. The supernatant was added to protease resistant 120 μl StrepTatcin Sepharose resin modified as previously described (Rafiee et al, MSB, 2020) and incubated on a rotating wheel for 60 minutes at 4 °C. The beads were loaded onto a 1 μm glass filter column and washed 3 times with 1 ml RIPA buffer, 3 times with 1 ml HNN buffer, and 3 times with 100 mM ammonium bicarbonate. Samples were transferred to a 10 kDa cutoff plate and centrifuged at 1500x g for 15 minutes. To the samples, 100 μl of 8 M urea was added. Tryptic digest Samples were reduced with 5 mM TCEP for 40 minutes at 37 °C and 200 rpm and alkylated with 40 mM IAA for 30 minutes at 30 °C in the dark, at 200 rpm. 1 μg Lys-C and 1 μg trypsin was added and samples were incubated overnight at 37 °C and 200 rpm. The digestion was stopped with 2% formic acid. Desalting Samples were desalted using HNFR S18V desalting plates according to manufacturer’s protocol. Samples were eluted twice with 200 μl Buffer B and dried in a vacuum centrifuge. Mass spectrometry AP-LiP-MS, AP-MS and mutant proximity labeling experiments were measured on an Orbitrap Fusion Lumos Tribrid mass spectrometer equipped with an Acquity M-Class UPLC System. Proximity labeling samples were measured on an Orbitrap Exploris 480 mass spectrometer equipped with an EASY-nLC 1000 System. Library samples consisting of pools of replicates were measured by DDA. Samples for quantification were measured by DIA."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Spectra were searched using Spectronaut v. 19 with directDIA separately for each experiment and bait. For AP-LiP-MS and AP-MS data, semi-specific peptides were included, and phosphorylation was included as a variable modification. For proximity labeling data, only specific peptides were included in the search, and the number of missed cleavages was set to four. Both biotinylation and phosphorylation were included as variable modifications and cross-run normalization was turned off. Report files were exported for further analysis."],"omics_type":["Proteomics"],"labhead":["Matthias Gstaiger"],"instrument_platform":[""],"labhead_affiliation":["Institute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["reberv@ethz.ch"],"publication":["Not available"],"submitter_affiliation":["IMSB, ETH Zurich"],"submitter_country":["Switzerland"],"additional_accession":[]},"is_claimable":false,"name":"Paradoxical non-catalytic kinase functions are driven by inhibitor-induced displacement of autoinhibitory domains","description":"Protein kinases are crucial regulators of cellular processes, and their dysregulation is frequently associated with human disorders. ATP-competitive type I inhibitors are widely used to block aberrant kinase activity. However, their effect on non-catalytic kinase functions such as conformation and protein-protein interactions (PPIs) remain largely uncharacterized. Here we present a multi-proteomics strategy to systematically measure these changes. First, we developed affinity purification (AP) and limited proteolysis coupled to mass spectrometry (AP-LiP-MS) to measure structural changes at high sequence coverage. We benchmarked AP-LiP-MS using DCLK1 before analyzing structural changes upon probe binding to CAMKK2, CHEK1, and PRKCA. All kinases underwent structural changes consistent with dissociation of domain-domain interactions (DDIs) between the kinase domain (KD) and the autoinhibitory domain (AID). Next, we applied AP and in vivo proximity labeling to analyze changes in kinase PPI networks. This revealed extensive and characteristic rewiring of functionally important PPIs, independent of catalytic activity. For instance, SCG-CAMKK2-1 binding to CAMKK2 sequestered PRKAA1, inhibiting its regulation by other kinases, while rabusertib caused CLPB-CHEK1 dissociation and mitochondrial fragmentation, and Gö 6983 resulted in PRKCA recruitment to cellular junctions. We propose that these unexpected phenotypes originate from on-target, off-mechanism effects, driven by structural changes and PPI rewiring. We advocate for the use of our workflow to systematically characterize overlooked consequences of small-molecule binding during drug development.","dates":{"publication":"2026-06-17","submission":"2025-10-23"},"accession":"PXD069830","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: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:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","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: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: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:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","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:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","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:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","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:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","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:51338","NEWT:575412","NEWT:28112","NEWT:6493","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:8655","NEWT:5147","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","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:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:231490","NEWT:244704","NEWT:7725","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:72664","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:4524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