{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/proteinGroups.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/20181016_SEL_LU_SA_CRN_R05_270918_IgGs_r01_C01_005.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/20181016_SEL_LU_SA_CRN_R05_270918_IgGs_r01_A02_001.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/20181016_SEL_LU_SA_CRN_R05_270918_IgGs_r02_C02_002.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/20181016_SEL_LU_SA_CRN_R05_270918_IgGs_r03_E02_003.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/20181016_SEL_LU_SA_CRN_R05_270918_p62_r01_B02_007.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/20181016_SEL_LU_SA_CRN_R05_270918_p62_r03_F01_012.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/20181016_SEL_LU_SA_CRN_R05_270918_IgGs_r01_A01_004.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/20181016_SEL_LU_SA_CRN_R05_270918_p62_r01_B01_010.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/20181016_SEL_LU_SA_CRN_R05_270918_p62_r02_D01_011.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/20181016_SEL_LU_SA_CRN_R05_270918_p62_r02_D02_008.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/20181016_SEL_LU_SA_CRN_R05_270918_p62_r03_F02_009.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/20181016_SEL_LU_SA_CRN_R05_270918_IgGs_r03_E01_006.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/Gel-Images.PNG","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065587/MaxQuant_txt.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["k.ryan@crukscotlandinstitute.ac.uk"],"submitter":["Sergio Lilla"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Gel-based experiment"],"disease":["Inflammation","Cancer"],"software":[""],"submitter_keywords":["Caspase","Inflammation","Autophagy","Tnf","P62","Protein cleavge","Apoptosis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065587"],"tissue":["Prostate Gland"],"sample_protocol":["Immunoprecipitation and LC-MS of tr-p62 LNCaP cells overexpressing wild-type p62 (pLX304 p62 WT) were treated with TNF (5ng/ml) for 24 hours. Cells were harvested in immunoprecipitation lysis buffer (20mM Hepes-KOH, 150mM NaCl, 1% Triton X-100, 2mM EDTA and Halt protease Inhibitor cocktail, Thermo Scientific, 78429) and proteins were isolated by centrifugation. Protein lysates were incubated with IgG control or p62 antibodies (1µg) at 4°C overnight. 50µl of Dynabeads Protein G were added the next day to each sample and rotated for 3 hours at 4°C. Beads were washed three times with immunoprecipitation wash buffer (20mM Hepes-KOH, 150mM NaCl, 1% Triton X-100, 2mM EDTA, 0.05% NP-40). Immunoprecipitated proteins were eluted by boiling the Dynabeads for 5min in IP-elution buffer (immunoprecipitation lysis buffer + 1x sample buffer for SDS-PAGE). Eluted proteins were then run on a polyacrylamide gel to separate full length and cleaved p62. Gel was stained with Instant Blue (Expedeon, ISB1L) to visualise proteins on the gel.  Proteolytic digestion of proteins ‘in gel’ The region on the gel containing the full length and cleaved p62 band were excised and washed twice with 50 mM ammonium bicarbonate, and 50 mM ammonium bicarbonate with 50% acetonitrile. Proteins in the gel bands were then reduced using dithiothreitol (10mM at 54°C for 30 minutes) and subsequently alkylated with iodoacetamide (55mM at room temperature for 45 minutes). Gel pieces were washed again with 50 mM ammonium bicarbonate; 50 mM ammonium bicarbonate with 50% acetonitrile; and finally dehydrated using acetonitrile before drying in a SpeedVac. Trypsin (5 µg/ml trypsin gold; Promega in 25 mM ammonium bicarbonate) was added and incubated for 16 h at 35 °C.  Tryptic peptides were extracted from gel pieces with two washes of 50% (v/v) acetonitrile/water + 1% trifluoroacetic acid (TFA) and subsequently dried in a SpeedVac. Dried peptides were resuspended in 0.1% TFA and  desalted using StageTip [Rappsilber 2007].  Mass Spectrometry Analysis Peptides resulting from digestions were separated by nanoscale C18 reverse-phase liquid chromatography using an EASY-nLC II 1200 (Thermo Scientific) coupled to an Orbitrap Fusion Lumos mass spectrometer (Thermo Scientific).  Elution was carried out at a flow rate of 300? nl/min using a binary gradient, into a 50?cm fused silica emitter (New Objective) packed in-house with ReproSil-Pur C18-AQ, 1.9?µm resin (Dr Maisch GmbH), for a total run-time duration of 85 minutes.  Packed emitter was kept at 50?°C by means of a column oven (Sonation) integrated into the nanoelectrospray ion source (Thermo Scientific). Eluting peptides were electrosprayed into the mass spectrometer using a nanoelectrospray ion source.  An Active Background Ion Reduction Device (ESI Source Solutions) was used to decrease air contaminants signal level.  The Xcalibur software (Thermo Scientific) was used for data acquisition.  A full scan over mass range of 350–1550 m/z was acquired at 60,000 resolution at 200 m/z. Higher energy collisional dissociation fragmentation was performed in the ion routing multipole, on the 15 most intense ions, and peptide fragments generated were analysed in the Orbitrap at 15,000 resolution."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The MS Raw data were processed with MaxQuant software [Cox 2008] version 1.6.3.3 and searched with Andromeda search engine [Cox 2011], querying SwissProt. First and main searches were performed with precursor mass tolerances of 20?ppm and 4.5?ppm, respectively, and MS/MS tolerance of 20?ppm. The minimum peptide length was set to six amino acids, and in order to identify C-term truncated peptides, MaxQuant digestion mode was set to “Unspecific”. Cysteine carbamidomethylation was set as fixed modification, whereas Methionine oxidation and N-terminal acetylation were specified as variable modifications. The peptide, protein, and site false discovery rate (FDR) was set to 1%.  All MaxQuant outputs were analysed with Perseus software version 1.6.15.0 [Tyanova 2016].   Peptide quantitation was performed using the intensity values reported in the modificationSpecificPeptides.txt file. Only peptides quantified in all replicates in at least one group (lower or upper band) were considered for analysis, missing values were imputed separately for each column. To identify site of cleavage of p62 we use the peptide intensity difference, and a 5% FDR permutation-based Student’s t-test."],"omics_type":["Proteomics"],"labhead":["Kevin Ryan"],"instrument_platform":[""],"labhead_affiliation":["CRUK -CRUK Scotland Institute for Cancer Research - Switchback Rd, Bearsden, Glasgow G61 1BD - United Kingdom"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["s.lilla@beatson.gla.ac.uk"],"publication":["10.1016/J.MOLCEL.2026.03.013"],"submitter_affiliation":["Proteomics"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Species-specific cleavage of the autophagy adaptor p62 dictates responses to TNF","description":"Inflammation is a driver of many diseases including cancer.  Several studies have also shown that changes to macroautophagy can affect inflammation.  We were interested in these connections and we report here that the autophagy adaptor proteins p62/SQSTM1 is cleaved upon treatment with the inflammatory cytokine TNF.  Mass spectrometry and CRISPR analysis revealed this cleavage occurs at D329 and is mediated by caspase-8, to produce a short form of p63, which we term tr-p62.  Our further analysis showed that cell death induced by TNF in the presence of Smac mimetics is not only dependent on p62, but intrinsically on its cleavage by caspase-8.  Moreover, as inhibition of autophagy causes p62 accumulation and sensitizes cell to death, we show that this effect is also dependent on the production of tr-p62.  Mechanistically, we show that tr-p62 is cleaved within and mediates a more stable caspase-8 activating complex, leading to a feed-forward loop of caspase-8 activation.  Surprisingly, however, we found that mice belong to a very small group of mammals in which this caspase-8 cleavage site in p62 is absent.  Introduction of either human p62 or a mutated cleavable version of mouse p62 into mouse cells renders them significantly more sensitive to cell death induced by TNF.  Furthermore, we used CRISPR/Cas9 technology to make p62 cleavable on mice and we show that these mice are intrinsically sensitive to treatment with TNF.  These findings therefore not only highlight a significant new step in the activation of cell death by TNF, but also provide a new mouse model that may provide better clarity for studies of mouse models of inflammatory 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