{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/CCDC114_DIA_labelfree_maxQvalue.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/16_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/23_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/14_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/17_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/15_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/23_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/13_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/16_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/14_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/14_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/13_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/23_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/15_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/17_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/17_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/13_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/15_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/16_3.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064456/Sample_Legend_and_LC-MS_Settings.docx"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["sxie@zju.edu.cn"],"submitter":["Feng Yang"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Human","Organoids","Ccdc114","Airway"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD064456"],"sample_protocol":["Total proteome extracted from 12-well plate-transwell ALI organoids (3 repeats) by lysing with TBSN buffer (20 mM Tris-HCl, pH8.0, 150 mM NaCl, 0.5% NP-40, 5 mM EGTA, 1.5 mM EDTA, 0.5 mM Na3VO4, and 20 mM p-nitrophenyl phosphate) supplementing with protease inhibitor cocktail (Roche, cat# 04693132001) for 30 min on ice. Protein concentration was determined using a bicinchoninic acid (BCA) assay kit, following the manufacturer’s protocol. 2.1 Aliquots containing 100 μg of protein were mixed with 20 μL of 20 mmol/L tris(2-carboxyethyl)phosphine (TCEP) solution, vortexed thoroughly, and incubated at 60℃ for 1 hour to achieve complete reduction. Following reduction, 10 μL of 200 mmol/L chloroacetamide (CAA) solution was added in the dark, followed by vigorous vortexing. The alkylation reaction was allowed to proceed for 30 minutes under light-protected conditions. For disulfide bond reduction, 5 μL of 20 mmol/L tris(2-carboxyethyl)phosphine (TCEP) solution was added under light-protected conditions, followed by thorough vortex mixing. The reduction reaction was allowed to proceed for 15 minutes in the dark at room temperature (25 ± 2°C). For protein precipitation, a 3:1 (v/v) ratio of ice-cold acetone (−20°C pre-chilled) was added to the sample. The mixture was incubated at −20°C for 4 hours to ensure complete precipitation. Following precipitation, samples were centrifuged at 1,500 × g for 10 min at 4°C. The supernatant was carefully discarded, and the pellet was air-dried to remove residual acetone. The precipitated pellet was resuspended in 50 μL of ice-cold acetone. The sample was then centrifuged at 3,500 × g for 10 min (4°C), followed by careful removal of the supernatant and the pellet was air-dried to remove residual acetone. The precipitated protein pellet was resuspended in 150 μL of 0.1 mol/L ammonium bicarbonate buffer (ABB, pH 8.0). Proteolytic digestion was performed by adding 4 μL of 1 mg/mL sequencing-grade trypsin (enzyme-to-protein ratio 1:25, w/w), followed by incubation at 37°C for 12-16 hour (overnight). The enzymatic digestion was quenched by adding 6 μL of 10% (v/v) trifluoroacetic acid (TFA) to achieve a final concentration of ~0.4% TFA (pH ≈ 3), effectively terminating trypsin activity. Prior to sample loading, SOLA™ SPE cartridges were sequentially activated with 200 μL of acetonitrile (ACN) and equilibrated with 200 μL of 0.1% (v/v) trifluoroacetic acid (TFA) in ultrapure water. Each step was followed by centrifugation at 100 × g for 1 min at 4℃ to remove the liquid phase. A 75 μL aliquot of the tryptic digest was loaded onto the preconditioned column and centrifuged at 40 × g for 2 min at 4°C. This loading process was repeated once  to ensure maximal peptide binding. The SPE cartridge was washed sequentially with three aliquots of 100 μL aqueous solution containing 0.1% (v/v) trifluoroacetic acid (TFA). Each wash step was followed by centrifugation at 60 × g for 1 min at 4°C to remove residual contaminants. Sequential elution was performed with two aliquots of 50 μL 60% acetonitrile (ACN) containing 0.1% (v/v) trifluoroacetic acid (TFA), followed by two aliquots of 50 μL 80% ACN/0.1% TFA. Each elution step was centrifuged at 40 × g for 2 min at 4°C. The combined 200 μL eluate was concentrated to dryness using a vacuum centrifugal concentrator. The dried peptides were reconstituted in 10–20 μL of 0.1% (v/v) formic acid (FA) in ultrapure water, followed by thorough vortex mixing, and centrifuged at 13,800 × g for 10 min at 4°C. The supernatant was carefully transferred to an LC-MS autosampler vial for analysis. Each sample was analysed on an Orbitrap HF (Thermo) that was coupled to an EASY-nLC 1200 liquid chromatography (LC) system (Thermo). The LC was operated in the one-column mode. The analytical column was a fused silica capillary (150 µm × 25 cm) with an integrated fritted emitter (15 µm; CoAnn Technologies) packed in-house with C18-AQ 1.9 µm resin (Thermo). The LC was equipped with two mobile phases: solvent A (0.1% formic acid, FA, in water) and solvent B (0.1% FA, 19.9% water and 80% acetonitrile, ACN). All solvents were of UPLC grade (Merk). Peptides were directly loaded onto the analytical column with a maximum flow rate that would not exceed the set pressure limit of 980 bar (usually around 0.6 – 1.0 µL/min). Peptides were subsequently separated on the analytical column by running a gradient of solvent A and solvent B. The exact composition of the gradient and the settings for the mass spectrometers can be found in the Sample_Legend_and_LC-MS_Settings.docx."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["RAW spectra were changed to mzML data by MSconvert, and search in DIA-NN (1.8.0) with label-free quantification. The MS/MS spectra data were searched by human fasta. The searches allowed oxidation of methionine residues (16 Da) and acetylation of the protein N-terminus (42 Da) as dynamic modification. Carbamidomethylation on Cysteine (57 Da) was set as static modification. Enzyme specificity was set to “Trypsin/P specific”. The instrument type was set to Orbitrap and the precursor mass tolerance was set to ±10 ppm (first search) and ±5 ppm (main search). The MS/MS match tolerance was set to ±0.5 Da. The peptide spectrum match FDR and the protein FDR were set to 0.01 (based on target-decoy approach). Minimum peptide length was 5 amino acids and maximum amino acid length 25. For protein quantification unique and razor peptides were allowed. Modified peptides were allowed for quantification. Label-free protein quantification was switched on, and unique and razor peptides were considered for quantification with a minimum ratio count of 1."],"omics_type":["Proteomics"],"labhead":["Shanshan Xie"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Children's Hospital, Zhejiang University School of Medicine, National Clinical Research Center for Child Health, Hangzhou, Zhejiang 310052, China"],"species":["Homo Sapiens (human)"],"publication":["41916967 Huo C, Luo T, Yang S, Jiang Y, Guo M, Yang F, Xu Z, Xia J, Wu L, Xu W, Gui M, Zhou T, Xie S. Loss-of-function variants in ODAD1 disrupt ODA docking and induce actin cytoskeletal remodeling in primary ciliary dyskinesia. Cell Discov. 2026 12(1):25 10.1038/s41421-026-00875-8"],"submitter_mail":["11718062@zju.edu.cn"],"submitter_affiliation":["Children’s Hospital, Zhejiang University School of Medicine, National Clinical Research Center for Child Health"],"submitter_country":["China"],"pubmed_abstract":["Primary ciliary dyskinesia (PCD) is a genetically heterogeneous disorder characterized by defective mucociliary clearance due to impaired motile cilia function. Outer dynein arm docking complex subunit 1 (ODAD1) encodes a structural component of the outer dynein arm docking complex (ODA-DC), which is crucial for effective ciliary beating. However, the full spectrum of ODAD1-associated pathogenesis remains incompletely defined. Here, we identified one novel homozygous loss-of-function ODAD1 variant, c.705_706insGCAG, and a recurrent homozygous splicing variant, c.-41-2A > C, in seven unrelated patients. These patients exhibited hallmark PCD symptoms with reduced nasal nitric oxide levels and situs inversus. Patient-derived nasal epithelial cells and air‒liquid interface (ALI) cultures exhibited a markedly reduced ciliary beating frequency and severe motility defects. Transmission electron microscopy and cryo-electron microscopy showed a complete loss of outer dynein arms and docking complexes, with variant-specific ultrastructural abnormalities. Unexpectedly, ODAD1 deficiency also led to reduced multiciliated cells (MCCs) abundance, misoriented basal bodies, and impaired multiciliogenesis. Proteomic profiling and immunostaining revealed prominent actin cytoskeletal remodeling, including aberrant F-actin bundling throughout the epithelial layers. Pharmacological inhibition of actin polymerization using cytochalasin B partially rescued the abundance of MCCs and multiciliogenesis, indicating that actin dysregulation is a modifiable consequence of ODAD1 loss. Finally, lentiviral re-expression of wild-type ODAD1 in patient-derived organoids restored ODA assembly and rescued coordinated ciliary beating, confirming the pathogenicity of the identified variants. Our data reveal a dual role for ODAD1 in regulating both axonemal structure and epithelial cytoskeletal integrity and identify actin dysregulation as a previously unrecognized, targetable pathological mechanism of ODAD1-associated PCD."],"pubmed_title":["Loss-of-function variants in ODAD1 disrupt ODA docking and induce actin cytoskeletal remodeling in primary ciliary dyskinesia."],"pubmed_authors":["Huo Chunxiao C, Luo Ting T, Yang Shuo S, Jiang Yuan Y, Guo Mengzhe M, Yang Feng F, Xu Zhangqi Z, Xia Junhua J, Wu Lei L, Xu Weize W, Gui Miao M, Zhou Tianhua T, Xie Shanshan S"],"additional_accession":[]},"is_claimable":false,"name":"Human CCDC114-mutant patient derived air-liquid interface (ALI) organoids proteome","description":"In this experiment we investigate the different expressed proteins between healthy control ALI organoids and CCDC114-mutant ALI 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