{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report.gg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report-first-pass.gg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report.pg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report.pr_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report.unique_genes_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report-first-pass.unique_genes_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report-first-pass.pr_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report.stats.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report-first-pass.stats.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report-first-pass.pg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report-first-pass.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report.log.txt"],"Pdf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/report.pdf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/miniT-SMARCA-BD-DMSO-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/miniT-SMARCA-BD-Cmpd1-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/miniT-SMARCA-BD-Cmpd3-R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/miniT-SMARCA-BD-Cmpd1-R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/miniT-SMARCA-BD-DMSO-R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/miniT-SMARCA-BD-Cmpd3-R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/miniT-SMARCA-BD-Cmpd1-R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/miniT-SMARCA-BD-Cmpd3-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/miniT-SMARCA-BD-DMSO-R1.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065523/session1.sps"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["a.ciulli@dundee.ac.uk"],"submitter":["Gajanan Sathe"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":["Not available"],"submitter_keywords":["E3 ligases ","Smarca2/4","Protein degrader"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065523"],"tissue":["Kidney Cell"],"sample_protocol":["Flp-In™ T-REx™ 293 stable cell line containing miniTurbo SMARCA2 Bromodomain was divided into three treatment conditions, with each condition consisting of three 10-cm dishes at ~70% confluency. Expression of the fusion protein was induced by 1 µg ml−1 doxycycline (Dox) treatment for a total of 20,5 hours. 12 hours after Dox induction, cells were then pre-treated with 10 µM MLN4924 Neddylation inhibitor (5054770001,Merck) for 30 mins followed by addition of 10 µM Compound1, 10 µM Compound3 or DMSO for 8 hours. Biotin (100 µM final concentration) was added to cells undergoing treatment with compounds or DMSO for 2 hours. At the endpoint, the culture medium was removed, and cells were collected with PBS by scraping in 15-cm tubes pelleted by centrifugation at 600g for at least 5 min. After a second wash with PBS, cells were lysed with RIPA lysis and extraction buffer (25 mM Tris-HCl pH 7.6, 150 mM NaCl, 1% NP-40, 1% sodium deoxycholate, 0.1% SDS) (#89900,Thermo Fisher Scientific) supplemented with complete EDTA-free protease inhibitor cocktail (11873580001,Roche) and 1:1000 benzonase nuclease (70746-3, Sigma-Aldrich). Lysates were incubated at 4 °C for 15 minutes, then centrifuged at 13,000g for 15 minutes at 4 °C. Protein concentration was determined by bicinchoninic acid (BCA) assay as described above. 300 µg of protein lysate was then incubated with 30 µl of pre-cleared High Capacity Streptavidin Agarose beads (Pierce, 20359) and the mixture was incubated on a rotating wheel for 12 hours at 4 °C. Beads were pelleted by centrifugation at 800 rpm for 5 minutes and then transferred with 1 ml of lysis buffer to a fresh Eppendorf tube. Beads were washed 5 times with washing buffer (50 mM Tris-HCl, 0.5% NP-40) and eluted with 5% SDS.    Elutes were reduced using a final concentration of 10 mM Pierce DTT (A39255, Thermo Fisher Scientific) dissolveld in Triethylammonium bicarbonate buffer (TEABC) (T7408, Sigma Aldrich) at 60ºC for 30 mins. Then, tubes were incubated to room temperature for 20 mins in dark and diluted to 20 mM iodoacetamide (A39271, Thermo Fisher Scientific) dissolved with TEABC. Afterwards, samples were processed with S-Trap™ mini spin column (PROTIFI, C02-mini) according to manufacter´s instructions. Finally, tryptic digestion was performed by incubating the processed sample with 10 µg Pierce Trypsin Protease MS-grade (90058, Thermo Fisher Scientific) dissolved in 100 µl 100 mM TEABC overnight at 37 °C. Samples were then eluted from the column and transferred to a fresh Eppendorf tube. Columns were washed first with 0.15% Formic Acid and then with 50% Acetonitrile in 0.15% formic acid and pooled with the eluate. Finally, sample were lyophilized and resuspended in 1% formic acid.    The dried peptides were reconstituted in 1% formic acid and analyzed on an Orbitrap Astral mass spectrometer connected to a Thermo Fisher Scientific Vanquish Neo UHPLC. The peptides were enriched on a trap column and separated on an analytical column (Easy-Spray PepMap Neo C18, 2 μm, 75 μm x 150 mm) at 800 nl/min.  Chromatographic separation was performed using a gradient elution: 5% BufferA (0,1% Formic Acid) and 22.5% buffer B [90% ACN, 0,1% Formic Acid] at 14 minutes, ramped to 35% at 21 minutes, followed by a return to 9%. The total run time was 22.6 minutes. Data acquisition was performed in Data-Independent Acquisition (DIA) mode using the Astral analyzer. The MS data acquired in Orbitrap were operated with a fixed cycle time of 5 ms and with a full scan range of 380 to 980 m/z at a resolution of 240,000. The AGC was set to 500% and ion injection time is custom. Precursor ion selection width was kept at 4-Th and peptide fragmentation was achieved by Higher-energy collisional dissociation (HCD, normalized collision energy 25%). For DIA mode, scan range used 150 to 2000, AGC target was 500%, ion injection was custom, and detector was Astral."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Acquired raw files were processed using DIA-NN, version 1.8 (https://github.com/vdemichev/DIaNN). Human UniProt was used as the protein sequence database. Two missed cleavage and a maximum of two variable modifications per peptide were allowed (acetylation of protein N-termini and oxidation of methionine). Carbamidomethylation of cysteines was set as fixed modification. This data analysis was carried out using library-free analysis mode in DIA-NN with “deep learning-based spectra and RTs prediction” enabled. MBR was enabled. The search results were further processed in Perseus . The data were loaded in Perseus in .txt format. Replicates were grouped based on their annotation to (Compound1, Compound3, ACEI-2004 or DMSO).  The data were log₂-transformed and missing values were imputed from a normal distribution using the “Processing → Imputation → Replace missing values from normal distribution” function in Perseus. Imputation parameters included a width of 0.3 and a downshift of 1.8 standard deviations, simulating low-abundance values to replace missing entries. The imputation was applied in 'whole matrix' mode. The processed data were subsequently used to generate volcano plots in GraphPad Prism (v9.5.1)."],"omics_type":["Proteomics"],"labhead":["Alessio Ciulli"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Professor • Centre for Targeted Protein Degradation"],"species":["Homo Sapiens (human)"],"publication":["42120501 Spiteri VA, Segal D, Correa-Sáez A, Iso K, Casement R, Muñoz I Ordoño M, Nakasone MA, Sathe G, Schätz C, Peters HE, Doward M, Kainacher L, Cowan AD, Ciulli A, Winter GE. Dual E3 ligase recruitment by monovalent degraders for tunable SMARCA 2/4 degradation. Nat Chem Biol. 2026 10.1038/s41589-026-02224-y"],"submitter_mail":["gsathe001@dundee.ac.uk"],"submitter_affiliation":["Centre for Targeted Protein Degradation (CeTPD)\nUniversity of Dundee"],"submitter_country":["United Kingdom"],"pubmed_abstract":["Proteolysis-targeting chimeras (PROTACs) and molecular glue degraders (MGDs) target proteins for degradation by co-opting an E3 ligase. While heterotrivalent PROTACs that can recruit multiple E3 ligases have been described, all MGDs reported to date depend on a single E3. Using orthogonal genetic screening, biophysical and structural analyses, we show that a monovalent MGD can recruit CUL4<sup>DCAF16</sup> and CRL1<sup>FBXO22</sup> in parallel to degrade SMARCA2/4. Deep mutational scanning identifies C173 in DCAF16 as essential for degrader activity and intact protein mass spectrometry confirms covalent modification at this site. Elucidating the ternary complex structure reveals a unique binding mode and a distinct interface of neointeractions that underlie degrader specificity. We demonstrate that ligase dependency is chemically and genetically tunable. Minimal compound modifications shift preference from DCAF16 to FBXO22, while a single substitution boosts degrader dependency on DCAF16. These results establish a framework for designing tunable dual E3 ligase degraders to mitigate potential resistance mechanisms."],"pubmed_title":["Dual E3 ligase recruitment by monovalent degraders for tunable SMARCA 2/4 degradation."],"pubmed_authors":["Spiteri Valentina A VA, Segal Dmitri D, Correa-Sáez Alejandro A, Iso Kentaro K, Casement Ryan R, Muñoz I Ordoño Miquel M, Nakasone Mark A MA, Sathe Gajanan G, Schätz Caroline C, Peters Hannah E HE, Doward Mark M, Kainacher Lisa L, Cowan Angus D AD, Ciulli Alessio A, Winter Georg E GE"],"additional_accession":[]},"is_claimable":false,"name":"SMARCA2/4 degradation tails mediate recruitment of two different E3 ligases ","description":"In this work, we characterise novel SMARCA2/4 degraders using a robust cell biology and structural workflow and reveal for the first time, the recruitment of two E3 ligase substrate receptors: FBXO22 and DCAF16 by the same degradation tail. Furthermore, we were able to chemically fine-tune this dual ligase dependency dialling out DCAF16 providing insights into the mechanisms for DCAF16 and FBXO22 covalent recruitment. Dual ligase recruitment may serve to overcome E3 ligase acquired resistance that may feature with clinical use of degraders.","dates":{"publication":"2026-05-16","submission":"2025-06-26"},"accession":"PXD065523","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","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: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: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: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:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","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: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: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:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:4232","NEWT:416348","NEWT:11298","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:72664","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:452467","NEWT:198822","NEWT:36111","NEWT:326424","NEWT:1678078","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:150847","NEWT:431947","NEWT:69014","NEWT:142809","NEWT:302409","NEWT:130821","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