{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/Ev_Rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/Ev_Rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/ElonC_HeCe_Rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/ElonC_HeCe_Rep3_20240323024415.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/ElonC_HeCe_Rep2_20240322215621.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/Ev_Rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/Ev_Rep2_20240322094129.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/Ev_Rep1_20240322055801.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/ElonC_HeCe_Rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/Ev_Rep3_20240322132457.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/ElonC_HeCe_Rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/ElonC_HeCe_Rep1_20240322170829.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD062976/RESULTS.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["luca.lignitto@inserm.fr"],"submitter":["AUDEBERT Stephane"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Bottom-up proteomics"],"disease":["Lung Cancer"],"software":["Not available"],"submitter_keywords":["cullin-ring ubiquitin ligase","Lc-msms; dia; elongin-c; elongin-b; cul2; cullin-ring ubiquitin ligase; crl2","Lc-msms","cul2","elongin-c","crl2","dia","elongin-b"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062976"],"tissue":["Kidney Epithelial Cell"],"sample_protocol":["For this experiment were used human HEK293T cells. Cells were transfected for 24hrs with: 2XFLAG-2XSTREP tagged empty vector; 2XFLAG-2XSTREP tagged Elongin-C + MYC tagged Elongin-B. All samples are in triplicate. Immunopurification was performed using Strep-Tactin Sepharose (iba #2-1201-010). Elution  was performed using desthiobiotin (iba #2-1000-025). Elution buffer composition: 1x desthiobiotin; 50 mM ammonium bicarbonate. All samples were treated with a proteasome inhibitor MG132 for 3 hours. Final concentration for MG132 = 10 µM in DMSO. Enriched samples (n=3, biological replicates) were loaded on NuPAGE™ 4–12% Bis–Tris acrylamide gels according to the manufacturer’s instructions (Life Technologies). Protein migration was interrupted as soon as the proteins stacked in a single band. Protein-containing bands were stained with Imperial Blue (Pierce), cut from the gel and digested with high sequencing grade trypsin (Promega) before being analysed by mass spectrometry. Briefly, gel pieces were washed and destained using few steps of 100mM NH4HCO3. Destained gel pieces were shrunk with 100 mM ammonium bicarbonate in 50% acetonitrile and dried at RT. Protein spots were then rehydrated using 10mM DTT in 25 mM ammonium bicarbonate pH 8.0 for 45 min at 56°C. This solution was replaced by 55 mM iodoacetamide in 25 mM ammonium bicarbonate pH 8.0 and the gel pieces were incubated for 30 min at room temperature in the dark. They were then washed twice in 25 mM ammonium bicarbonate and finally shrunk by incubation for 5 min with 25 mM ammonium bicarbonate in 50% acetonitrile. The resulting alkylated gel pieces were dried at room temperature. The dried gel pieces were reswollen by incubation in 25 mM ammonium bicarbonate pH 8.0 supplemented with 12.5 ng/µl trypsin (Promega) for 1h at 4°C and then incubated overnight at 37°C. Peptides were harvested by collecting the initial digestion solution and carrying out two extractions; first in 5% formic acid, then in 5% formic acid in 60% acetonitrile. Pooled extracts were dried down in a centrifugal vacuum system. Peptides were further reconstituted in 15µl water/acetonitrile/ (98/2) containing 0.05%TFA. 10% of each sample was analyzed twice by liquid chromatography (LC)-tandem MS (MS/MS) using a Q-Exactive plus Mass Spectrometer (Thermo Fisher Scientific, San Jose, CA) online with a nanoRSLC Ultimate 3000 chromatography system (Thermo Fisher Scientific, Sunnyvale, CA). First, peptides were concentrated and purified on a pre-column PepMap100 C18, 2 cm × 100 μm I.D, 100 Å pore size, 5 μm particle size in solvent A (0.1% formic acid in 2% acetonitrile). In the second step, peptides were separated on a reverse phase LC EASY-Spray C18 column PepMap RSLC C18, 50 cm × 75 μm I.D, 100 Å pore size, 2 μm particle size (Thermo Fisher) at 300 nL.min−1 flow rate and 40°C. After column equilibration peptides were eluted from the analytical column by a three-step linear gradient (2.5%–27.5% solvent B [80% acetonitrile 0.1% formic acid in water] for 100 min, 27.5%–40% for 20 min and a last elution 40%–90% for 2 min). For peptide ionization in the EASY-Spray nanosource in front of the mass spectrometer, the spray voltage was set at 1,9 kV and the capillary temperature at 250°C. The mass spectrometer was used in data-independent acquisition (DIA) mode with the following parameters. First, MS spectra were acquired in the Orbitrap in the range of m/z 375–1500 at a FWHM resolution of 35,000 measured at 200 m/z. AGC target was set at 1 × 106 with a Maximum Injection Time of 60 ms. MS2 spectra were acquired in the Orbitrap with a resolution of 17,500 after isolation of the parent ion in the quadrupole and fragmentation in the HCD cell under collision Energy of 27%. DIA parent ion range was from 400 to 1000 m.z−1 divided into 24 m.z−1 windows."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Enriched samples (n=3, biological replicates) were loaded on NuPAGE™ 4–12% Bis–Tris acrylamide gels according to the manufacturer’s instructions (Life Technologies). Protein migration was interrupted as soon as the proteins stacked in a single band. Protein-containing bands were stained with Imperial Blue (Pierce), cut from the gel and digested with high sequencing grade trypsin (Promega) before being analysed by mass spectrometry. Briefly, gel pieces were washed and destained using few steps of 100mM NH4HCO3. Destained gel pieces were shrunk with 100 mM ammonium bicarbonate in 50% acetonitrile and dried at RT. Protein spots were then rehydrated using 10mM DTT in 25 mM ammonium bicarbonate pH 8.0 for 45 min at 56°C. This solution was replaced by 55 mM iodoacetamide in 25 mM ammonium bicarbonate pH 8.0 and the gel pieces were incubated for 30 min at room temperature in the dark. They were then washed twice in 25 mM ammonium bicarbonate and finally shrunk by incubation for 5 min with 25 mM ammonium bicarbonate in 50% acetonitrile. The resulting alkylated gel pieces were dried at room temperature. The dried gel pieces were reswollen by incubation in 25 mM ammonium bicarbonate pH 8.0 supplemented with 12.5 ng/µl trypsin (Promega) for 1h at 4°C and then incubated overnight at 37°C. Peptides were harvested by collecting the initial digestion solution and carrying out two extractions; first in 5% formic acid, then in 5% formic acid in 60% acetonitrile. Pooled extracts were dried down in a centrifugal vacuum system. Peptides were further reconstituted in 15µl water/acetonitrile/ (98/2) containing 0.05%TFA. 10% of each sample was analyzed twice by liquid chromatography (LC)-tandem MS (MS/MS) using a Q-Exactive plus Mass Spectrometer (Thermo Fisher Scientific, San Jose, CA) online with a nanoRSLC Ultimate 3000 chromatography system (Thermo Fisher Scientific, Sunnyvale, CA). First, peptides were concentrated and purified on a pre-column PepMap100 C18, 2 cm × 100 μm I.D, 100 Å pore size, 5 μm particle size in solvent A (0.1% formic acid in 2% acetonitrile). In the second step, peptides were separated on a reverse phase LC EASY-Spray C18 column PepMap RSLC C18, 50 cm × 75 μm I.D, 100 Å pore size, 2 μm particle size (Thermo Fisher) at 300 nL.min−1 flow rate and 40°C. After column equilibration peptides were eluted from the analytical column by a three-step linear gradient (2.5%–27.5% solvent B [80% acetonitrile 0.1% formic acid in water] for 100 min, 27.5%–40% for 20 min and a last elution 40%–90% for 2 min). For peptide ionization in the EASY-Spray nanosource in front of the mass spectrometer, the spray voltage was set at 1,9 kV and the capillary temperature at 250°C. The mass spectrometer was used in data-independent acquisition (DIA) mode with the following parameters. First, MS spectra were acquired in the Orbitrap in the range of m/z 375–1500 at a FWHM resolution of 35,000 measured at 200 m/z. AGC target was set at 1 × 106 with a Maximum Injection Time of 60 ms. MS2 spectra were acquired in the Orbitrap with a resolution of 17,500 after isolation of the parent ion in the quadrupole and fragmentation in the HCD cell under collision Energy of 27%. DIA parent ion range was from 400 to 1000 m.z−1 divided into 24 m.z−1 windows."],"omics_type":["Proteomics"],"labhead":["Luca Lignitto, PhD"],"instrument_platform":[""],"labhead_affiliation":["CRCM, INSERM, CNRS, Institut Paoli-Calmette, Aix-Marseille University, 27 Boulevard Leï Roure, 13009, Marseille, France"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["stephane.audebert@inserm.fr"],"publication":["42086045 Ahmed B, Salaun D, Jordan JB, Daulat A, Pastorello C, Brito T, Yang Y, Josselin E, Byrne D, Betzi S, Pelletier A, Vernerey J, Ferreira L, Castellano R, Audebert S, Camoin L, Pane A, Bechara C, Borg JP, Modesti M, Lignitto L. CRL2&lt;sup&gt;FEM1B&lt;/sup&gt; uses heme to recruit BACH1 for degradation and regulate ferroptosis in lung cancer. Mol Cell. 2026 86(10):1993-2011.e10 10.1016/j.molcel.2026.04.008"],"submitter_affiliation":["Marseille Proteomic, Centre de Recherche en Cancérologie de Marseille, Inserm UMR1068, CNRS UMR7258, Aix Marseille Université U105, Institut Paoli Calmettes, 27 Boulevard Leï Roure CS30059 13273 Marseille Cedex 09 France"],"submitter_country":["France"],"pubmed_abstract":["Lung cancers frequently increase iron demand to sustain growth, which makes them vulnerable to ferroptosis. While Cullin 2-RING ubiquitin ligases (CRL2s) are critical regulators of stress responses and redox balance, their role in ferroptosis mechanisms remains largely unknown. Here, we identify the E3 ligase CRL2<sup>FEM1B</sup> as a key regulator of the ferroptotic response. CRL2<sup>FEM1B</sup> recruits BTB and CNC homolog 1 (BACH1), a transcriptional regulator of ferroptosis, for degradation by recognizing a degron that is directly formed by the redox-sensing molecule heme. By degrading BACH1 in response to heme, CRL2<sup>FEM1B</sup> acts as a switch that dynamically modulates the transcriptional activation of ferroptosis-protective genes, particularly solute carrier family 7 member 11 (SLC7A11). Loss of CRL2<sup>FEM1B</sup> stabilizes BACH1 and suppresses SLC7A11, thereby sensitizing lung tumor cells to ferroptosis inducers in vitro and in preclinical models. Our findings identify CRL2<sup>FEM1B</sup> as a target to increase the efficacy of ferroptosis inducers in lung cancer treatment and define a broader principle whereby endogenous metabolites regulate protein degradation by enabling substrate-E3 ligase interactions."],"pubmed_title":["CRL2&lt;sup&gt;FEM1B&lt;/sup&gt; uses heme to recruit BACH1 for degradation and regulate ferroptosis in lung cancer."],"pubmed_authors":["Ahmed Bashir B, Salaun Daniele D, Jordan Jack B JB, Daulat Avais A, Pastorello Chiara C, Brito Tarcísio T, Yang Yuying Y, Josselin Emmanuelle E, Byrne Deborah D, Betzi Stephane S, Pelletier Amandine A, Vernerey Julien J, Ferreira Lorene L, Castellano Remy R, Audebert Stephane S, Camoin Luc L, Pane Attilio A, Bechara Cherine C, Borg Jean-Paul JP, Modesti Mauro M, Lignitto Luca L"],"additional_accession":[]},"is_claimable":false,"name":"Heme acts as a molecular degrader linking CRL2-FEM1B to substrate proteolysis and ferroptosis regulation in lung cancer","description":"In this project, we sought to identify the proteins interacting with the Elongin-C/Elongin-B complex. To this end, we performed affinity purification of Elongin-C and Elongin-B tagged with FLAG-STREP and MYC, respectively. A cell line with FLAG-STREP empty vector was used as negative control. 3 biological replicates were used for each sample group.","dates":{"publication":"2026-06-11","submission":"2025-04-15"},"accession":"PXD062976","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:5530","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:49928","NEWT:3349","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","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:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","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:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:321967","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:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","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:56870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