{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report-first-pass.unique_genes_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report-first-pass.stats.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report-first-pass.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report.pr_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report-first-pass.gg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report.stats.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report.gg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report-first-pass.pr_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report.unique_genes_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report.pg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report-first-pass.pg_matrix.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/report.log.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/gene58_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/gene58_15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/gene58_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/gene58_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/gene58_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/gene58_14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/gene58_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/gene58_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/gene58_2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065445/gene58_tp.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/PXD065445"],"tissue":["Kidney"],"sample_protocol":["For unbiased identification of degrader target proteins, 1 × 106 HEK-293 cells per condition were treated with DMSO (1:1,000), ACEI-2004 (1 µM) or GNE-58 (1 µM) for 12 h in biological triplicates. Cells were collected via centrifugation, washed two times in ice-cold PBS and cellular pellets were lysed in 100 µl of RIPA buffer supplemented with benzonase and cOmplete EDTA-free Protease Inhibitor Cocktail. Cell debris was removed by centrifugation at 13,000 rpm for 15 min at 4 °C. Supernatant was transferred to fresh tubes and protein concentration determined using the BCA protein assay kit . 50 m µg of cell lysate was then diluted to a final 5% SDS concentration and proteins were first reduced at 55ºC for 15 mins in DTT (A39255, Thermo Fisher Scientific) dissolveld in Triethylammonium bicarbonate buffer (TEABC) (T7408, Sigma Aldrich) to a final concentration of 5 mM. Proteins were alkylated with to a final 20 mM iodoacetamide (A39271, Thermo Fisher Scientific) dissolved with TEABC in the dark for 10 min at room temperature. Afterwards, samples were processed with S-Trap™ micro spin column (PROTIFI, C02-micro) 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 sample was analyzed on an Orbitrap Ascend Tribrid mass spectrometer coupled to a Thermo Fisher Scientific Vanquish Neo UHPLC. The peptides were enriched on a trap column and resolved on an analytical column (Easy-Spray PepMap Neo 2 μm C18 75 μm × 150 mm) with 800 nl/min. The gradient for separation was used as 2-7% B at 6 min, 7-18% at 89 min, 18-27% at 114 min, 27-35% at 134 min followed by column wash. Total run time used was 155 min.The data were acquired in data-independent acquisition mode in an orbitrap analyzer.  The MS data acquired in Orbitrap were operated with  standard AGC and auto ion injection time and with a full scan range of 300 to 1350 m/z at a resolution of 60,000. For DIA scan precurson mass range were used as 400-1000, precursor was isolated in quadrupole with isolation window 10 Th and peptide fragmentation was achieved by HCD (normalized collision energy 30%). The resolution was set s 15,000."],"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 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