{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/checksum.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/mqpar_DMSO_SEN177.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/mqpar_shCTR_shQPCT.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/20250419_PDIA4_IP_shQPCT_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/20250419_PDIA4_IP_shQPCT_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/20250419_pglu_sen177_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/20250419_pglu_sen177_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/20250419_PDIA4_IP_shCTR_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/20250419_PDIA4_IP_shCTR_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/20250419_pglu_dmso_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/20250419_PDIA4_IP_shQPCT_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/20250419_pglu_sen177_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/20250419_pglu_dmso_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/20250419_PDIA4_IP_shCTR_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069857/20250419_pglu_dmso_3.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["jyates@scripps.edu"],"submitter":["Le Sun"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Cystic Fibrosis"],"software":["Not available"],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069857"],"tissue":["Epithelial Cell","Cell Culture"],"sample_protocol":["Cells were harvested and lysed in 1% NP-40 buffer (25 mM Tris-HCl, pH 7.4, 150 mM NaCl, 1% protease inhibitor cocktail, 1% NP-40) at 4°C. Cell lysates were clarified by centrifugation at 14,000 × g for 15 min at 4°C. The supernatants were incubated with anti-FLAG M2 affinity resin (Sigma-Aldrich, M8823) for at 4°C for 4 hours with gentle rotation. After incubation, beads were washed extensively with 1% NP-40 buffer to remove nonspecific proteins. The FLAG beads were resuspended in 8 M urea (Sigma-Aldrich, U5128) in 100 mM TEAB (Thermo Fisher Scientific, 90114) and then incubated with 5 mM TCEP (Sigma-Aldrich, C4706) at room temperature for 30 minutes followed by 10 mM IAA (Sigma-Aldrich, I1149) with vortex at room temperature for 15 minutes in the dark. 100 mM TEAB was added to reduce the urea concentration to 2 M. Then 1 mM CaCl2 and 1 μg trypsin(Promega, V5113) were added for overnight digestion at 37 ˚C. The resulting peptides were acidified with 5% formic acid, desalted, and saved for further mass spectrometry analysis.Samples were loaded onto EvoTips (Evosep) in accordance with the manufacturer’s protocol and were analyzed by liquid chromatography tandem mass-spectrometry using an Orbitrap Fusion Lumos mass spectrometer (Thermo Fisher Scientific) coupled to an Evosep One system (Evosep). Peptides were separated on a C18 analytical column (100 μm × 25 cm, 5 μm tip) packed with 1.7 μm BEH beads (Waters) using a gradient of buffer A (0.1% formic acid in water) and buffer B (90% acetonitrile). Liquid chromatography separation was performed using an SPD method (15 samples per day). The voltage applied to nanoelectron spray ionization (nESI) source was 2.5 kV and the source temperature was 275 °C. Peptide spectra were acquired in the data-dependent acquisition (DDA) mode. Briefly, Full MS1 scans were collected in the Orbitrap at resolution 120,000. The cycle time was set to 3 seconds, and within these 3 seconds, the most abundant ions per scan were selected for collision-induced dissociation MS2 in Orbitrap. Monoisotopic precursor selection was enabled, and dynamic exclusion was used with an exclusion duration of 10 seconds."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Protein and peptide identification was done with Integrated Proteomics Pipeline (IP2, Bruker Scientific LLC). MS data were searched using the ProLuCID algorithm against a sequence database of UniProt SwissProt human reviewed proteome appended with the sequences of common contaminant proteins, and with the reverse sequences as decoy. The MS/MS spectra were searched and filtered using the following parameters: static modifications of carbamidomethylation (57.02146, cysteine), dynamic pyroglutamate modification (delta mass: -17.02) on glutamine or (delta mass: -18.01) on glutamic acid at N-terminal of peptide, precursor mass tolerance of 10 ppm, fragment ion mass tolerance 0.6 Da, one tryptic end (K/R), up to 3 missed cleavages, and minimum peptide length 4. Protein identification required that at least 1 peptide was identified per protein, and the data was filtered to a peptide and protein false discovery rate (FDR) less than 0.01 using the target-decoy method."],"omics_type":["Proteomics"],"labhead":["John Yates"],"instrument_platform":[""],"labhead_affiliation":["the Scripps Research Institute"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["lsun@scripps.edu"],"publication":["10.1038/S41467-026-74078-W"],"submitter_affiliation":["the Scripps Research Institute"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"QPCT-PDIA4 rescues ΔF508 and N1303K CFTR function  in cystic fibrosis","description":"Cystic fibrosis (CF) is a genetic disorder caused by CFTR mutations, most commonly ΔF508, leading to defective ion transport and multisystem pathology. Small-molecule modulators partially restore mutant CFTR function, but therapeutic efficacy remains limited, particularly for N1303K mutation refractory to current treatments. Here, we show that inhibition of the glutaminyl-peptide cyclotransferase (QPCT)-dependent pathway rescues both the surface expression and functional activity of ΔF508 CFTR. Integrated molecular and physiological analyses identify protein disulfide-isomerase A4 (PDIA4) as a key mediator of this rescue via its pyroglutamate (pGlu)-dependent interaction with ΔF508 CFTR, which is essential for surface trafficking. Furthermore, inhibition of QPCT also restores the function of the N1303K CFTR mutant, revealing a broader mechanistic relevance of this pathway in correcting CFTR misfolding and trafficking defects. These findings uncover a generalizable mechanism for correcting CFTR folding abnormalities and suggest new therapeutic strategies for mutations unresponsive to existing 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