{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/Seq92503_DIA_480Ex2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/Seq92505_DIA_480Ex2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/Seq92512_DIA_480Ex2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/Seq92510_DIA_480Ex2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/Seq92509_DIA_480Ex2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/Seq92507_DIA_480Ex2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/Seq92502_DIA_480Ex2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/Seq92504_DIA_480Ex2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/Seq92506_DIA_480Ex2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/Seq92513_DIA_480Ex2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/Seq92511_DIA_480Ex2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/Seq92508_DIA_480Ex2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069489/92502-13.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["itay.koren@biu.ac.il"],"submitter":["Keren Bendalak"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Ubiquitin","Protein degradation","E3 ligases","March5","Peroxisomal membrane proteins (pmps)","Peroxisome","Mul1","Protein quality control"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069489"],"sample_protocol":["Proteolysis  Cells were lyzed in 8.5M Urea, 400mM ammonium bicarbonate and 10mM DTT, sonicated twice (90%, 10-10, 5’), and centrifuged (10,000g, 10’). Protein amount was estimated using Bradford readings. The samples were reduced (60ºC for 30 min), modified with 35.2mM iodoacetamide in 100mM ammonium bicarbonate (room temperature for 30 min in the dark) and digested in 1.5M Urea, 66mM ammonium bicarbonate with modified trypsin (Promega), overnight at 37oC in a 1:50 (M/M) enzyme-to-substrate ratio. An additional second digestion with Trypsin was done for 4 hours at 37oC in a 1:100 (M/M) enzyme-to-substrate ratio. The tryptic peptides were desalted using Oasis HLB 96-well µElution Plate (Waters), dried and re-suspended in 0.1% Formic acid in 2% acetonitrile. mass spectrometry analysis The resulting peptides were analyzed by LC-MS/MS using an Exploris 480 mass spectrometer (Thermo) fitted with a capillary HPLC (Vanquish, Thermo scientific). The peptides were loaded in solvent A (0.1% formic acid in water) on an ionoptics, AUR3-25075C18-XT, 25cm x 75um ID, 1.7um C18 reversed phase analytical column. The peptides mixture was resolved with a 6 to 34% linear gradient of solvent B (80% acetonitrile with 0.1% formic acid) for 120 minutes followed by a 0.1min increase of 34 to 99% and 11 minutes at 99% solvent B at flow rates of 0.15 μl/min. Mass spectrometry was performed in a positive mode using repetitively full MS scan (m/z 380–985, resolution 120,000) followed by DIA scans (10Da isolation windows with 1 m/z overlap, and resolution 30,000)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The mass spectrometry data was analyzed using the DIA-NN software version 1.9.2 (1, 2) against human proteome from the Uniprot database (20662 entries, downloaded January 2025), with Min peptide length set to 7, Maximum number of missed cleavages set to 1, Cysteine carbamidomethylation enabled as a fixed modification, and protein N-term acetylation enabled as a variable modification. Peptide- and protein-level false discovery rates (FDRs) were filtered to 1%. Statistical analysis of the identification and quantization results was done using Perseus 1.6.7 software (3). References: 1) Demichev et al, Nature Methods, 2020, https://www.nature.com/articles/s41592-019-0638-x 2) analysing Scanning SWATH: Messner et al, Nature Biotechnology, 2021, https://www.nature.com/articles/s41587-021-00860-4 3) Stefka Tyanova, Tikira Temu, Pavel Sinitcyn, Arthur Carlson, Marco Y Hein, Tamar Geiger, Matthias Mann Jürgen Cox. The Perseus computational platform for comprehensive analysis of proteomics data. Nat Methods. 2016 Sep;13(9):731-40."],"omics_type":["Proteomics"],"labhead":["Itay Koren"],"instrument_platform":[""],"labhead_affiliation":["Bar-Ilan university, Israel"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["kerenb@technion.ac.il"],"submitter_affiliation":["Technion"],"submitter_country":["Israel"],"additional_accession":[]},"is_claimable":false,"name":"A Mitochondria-Driven Quality Control Pathway Eliminates Mislocalized Peroxisomal Membrane Proteins","description":"Protein quality control (PQC) systems are essential for maintaining a healthy proteome by removing aberrant proteins, including mislocalized proteins. However, the mechanisms for eliminating mislocalized Peroxisomal Membrane Proteins (PMPs) have remained elusive. Here, using quantitative proteomics in peroxisome biogenesis–deficient cells, we observed widespread downregulation of PMPs without corresponding changes in mRNA levels, indicating selective post-transcriptional turnover. An unbiased CRISPR screen uncovered an inter-organelle PQC axis in which mitochondria act as a surveillance hub to clear mislocalized PMPs, thereby safeguarding cellular proteostasis when peroxisome biogenesis fails. We show that when PMPs fail to reach their native peroxisomal destination, they are rerouted to mitochondria, where the mitochondrial outer membrane resident E3 ligases MUL1 and MARCH5 act redundantly to ubiquitinate them and promote their degradation via the proteasome. Our findings reveal an additional regulatory layer of organelle cross-talk, highlighting a dual role for mitochondrial E3 ligases, previously implicated in de novo peroxisome biogenesis, in actively participating in peroxisomal protein quality control. Notably, simultaneous loss of peroxisomes and mitochondrial E3 ligases markedly impairs cell survival, highlighting the essential role of this pathway. These findings provide critical insights into the pathology of organelle dysfunction, including peroxisome biogenesis disorders, and reveal broader mechanisms of inter-organelle protein quality 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