{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD062550/24-93-PRIDE-SampleList.xlsx"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD062550/Q25-24-93-01-12zebrafish.msf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD062550/Q25-24-93-09.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD062550/Q25-24-93-08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD062550/Q25-24-93-10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD062550/Q25-24-93-04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD062550/Q25-24-93-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD062550/Q25-24-93-02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD062550/Q25-24-93-11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD062550/Q25-24-93-05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD062550/Q25-24-93-06.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["m.luzarowski@zmbh.uni-heidelberg.de"],"submitter":["Marcin Luzarowski"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Heart","Mitochondria","Wash3","Proteomics","Zebrafish"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062550"],"sample_protocol":["Hearts were collected from 1-year-old adult zebrafish. Heart samples were homogenized using a tissue grinder (Cat# 947820B, Kisker Biotech, Germany) in 8 M Urea lysis buffer (8 M Urea, 50 mM Tris-HCL pH 8.0, 5 mM EDTA) and incubated on ice for 1 hour. Samples were centrifuged at 20,000 x g for 10 minutes. Cleared supernatants were subjected to determine protein concentration using Pierce™ BCA Protein Assay Kit (Thermo Scientific, Waltham, MA, USA).  Each samples contained 40 g of extracted protein and were precipitated using the Chloroform/Methanol method. Protein extracts were digested using the SP3 method with some modifications [ref: Single-pot, solid-phase-enhanced sample preparation for proteomics experiments]. Magnetic bead-based sample preparation was carried out using a prototype magnetic bead slurry (Promega, Cat. No. 916738). For each sample, 2 µL of Promega magnetic beads (100 mg/mL) were added and mixed with the protein solution by gentle pipetting. Protein binding was induced by the addition of 800 µL of 100% acetonitrile (ACN), resulting in a final concentration of 80% ACN. Samples were vortexed for 15 to 30 seconds to ensure homogeneity and incubated for 20 minutes at 24 °C with shaking at 1200 rpm. Following incubation, samples were briefly centrifuged to collect liquid from the tube lid and then placed on a magnetic rack to separate the beads. The supernatant was removed and discarded. Bound proteins were washed three times with 1 mL of 80% ethanol and once with 1 mL of 80% ACN. Beads were collected on the magnetic rack, the wash solution was completely removed, and the beads were air-dried for 1 minute. Beads were reconstituted in 100 µl of 100 mM TEAB pH 8.5. Trypsin was added in a ratio of 1:50, followed by overnight incubation at 37°C. Samples were acidified using TFA to reach pH < 2. The pH of each sample was verified to be <2 before proceeding to StageTip desalting and LC-MS analysis. Digested proteins were desalted on self-assembled C18 Empore® extraction discs (3M, Maplewood, MN) [ref: Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips]. Samples were suspended in 0.1% TFA and analyzed using an Ultimate 3000 liquid chromatography system coupled to an Orbitrap QE HF (Thermo Fisher) as described before [cite: 3-Mercaptopyruvate sulfur transferase is a protein persulfidase (2023)]. Briefly, peptides were separated in a 120 min linear gradient starting from 3% B and increasing to 23% B over 100 min and to 38% B over 20 min, followed by washout with 95% B. The mass spectrometer was operated in data-dependent acquisition mode, automatically switching between MS and MS2. MS spectra (m/z 400–1600) were acquired in the Orbitrap at 60,000 (m/z 400) resolution and MS2 spectra were generated for up to 15 precursors with a normalized collision energy of 27 and an isolation width of 1.4 m/z."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The MS/MS spectra were searched against the UniProt D. rerio UP000814640 (August 2022), and a customized contaminant database using Proteome Discoverer 2.5 with Sequest HT (Thermo Fisher Scientific). The fragment ion mass tolerance was set to 0.02 Da and the parent ion mass tolerance to 5 ppm. Trypsin was specified as an enzyme. The following variable modifications were allowed: Oxidation (M), Deamidation (N, Q), Acetylation (N-term), Met-loss (M), Met-loss+Acetyl (N-Term), whereas Carbamidomethylation (C) was set as a fixed modification. Peptide quantification was done using a precursor ion quantifier node with the Top N Average (n = 3) method set for protein abundance calculation. Perseus software (version, 2.0.11) was used for processing the result of proteomic analysis. All values were log2 transformed and filtered rows based on all three values identified at least one group. Missing values were replaced from a normal distribution for each replicate and differentially expressed proteins verified by ANOVA (Threshold, p<0.05)."],"omics_type":["Proteomics"],"labhead":["Marcin Luzarowski"],"instrument_platform":[""],"labhead_affiliation":["Core Facility for Mass Spectrometry and Proteomics, Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, 69120 Heidelberg, Germany"],"submission_type":["PARTIAL"],"species":["Danio Rerio (zebrafish) (brachydanio Rerio)"],"submitter_mail":["m.luzarowski@zmbh.uni-heidelberg.de"],"publication":["41768586 Kim S, Park DD, Glazier A, Rottbauer W, Just S. WASHC3 knockout disrupts mitochondrial protein homeostasis and energy metabolism in cardiomyocytes. Front Cardiovasc Med. 2026 13:1682381 10.3389/fcvm.2026.1682381"],"submitter_affiliation":["University of Heidelberg"],"submitter_country":["Germany"],"pubmed_abstract":["<h4>Introduction</h4>The WASH complex regulates endosomal actin dynamics and vesicular trafficking and is essential for neuronal integrity and motor function. Although variants in WASHC4, WASHC5, and WASHC3 are linked to neurodevelopmental abnormalities, the role of WASHC3 beyond the nervous system, particularly in cardiac mitochondrial regulation, remains unclear.<h4>Methods</h4>We modeled WASHC3 loss of function in zebrafish and human cardiomyocytes. Washc3 was suppressed in zebrafish embryos by antisense oligonucleotide-mediated knockdown, and a stable Washc3 knockout line was generated using CRISPR/Cas9. Washc3-deficient zebrafish hearts were analyzed by quantitative LC-MS/MS proteomics with GO/KEGG enrichment and transcript-level assays. Mitochondrial bioenergetics was assessed by Seahorse XF assays in primary zebrafish cardiomyocytes and in human AC16 cardiomyocytes following AAV-shRNA-mediated WASHC3 knockdown.<h4>Results</h4>Washc3 knockdown embryos exhibited neuromuscular degeneration, impaired locomotion, and early cardiac dysfunction. In contrast, Washc3 knockout zebrafish showed normal early development but developed progressive pericardial degeneration and epicardial remodeling in aged animals. Cardiac proteomics revealed downregulation of mitochondrial proteins, particularly oxidative phosphorylation components, supported by pathway enrichment and concordant transcript-level findings. Mitochondrial respiration was significantly impaired in both Washc3-deficient zebrafish cardiomyocytes and WASHC3-depleted human AC16 cardiomyocytes.<h4>Discussion</h4>These findings identify a previously unrecognized role for WASHC3 in maintaining cardiac mitochondrial protein homeostasis and bioenergetic function and provide a framework linking neuromuscular and cardiac phenotypes to impaired mitochondrial bioenergetics in energy-demanding tissues."],"pubmed_title":["WASHC3 knockout disrupts mitochondrial protein homeostasis and energy metabolism in cardiomyocytes."],"pubmed_authors":["Kim Sujin S, Park Deung-Dae DD, Glazier Amelia A, Rottbauer Wolfgang W, Just Steffen S"],"additional_accession":[]},"is_claimable":false,"name":"A proteomic analysis of WASH complex subunit 3 deficiency in adult heart.","description":"The WASH complex is primarily responsible for the activation of actin branching on endosomes, regulating vesicle trafficking across intracellular organelles. As one of the core subunits of the WASH complex, the function of washc3 remains largely unknown. In this study, we performed proteomic analysis of washc3 mutant, focusing specifically on the adult 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