{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_14Plex_TMT_Synaptosomes_PS.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_9.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/040324_Synaptosomes_Fraction_2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064880/px-submission-tool-2.10.0.jar.jar"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["pete.cullen@bristol.ac.uk"],"submitter":["Kohji Kato"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Vps35l","Synapsin1","Synaptosome","Lc-ms/ms","Tmt label"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD064880"],"tissue":["Brain"],"sample_protocol":["Synaptosome preparation. The mice were deeply anesthetized with isoflurane, decapitated, and perfused with PBS. The hippocampus was harvested under a microscope on postnatal day 7, followed by synaptosome isolation as previously described(64). Briefly, each hippocampus was transferred to a glass homogenizer and Syn-PER reagent was added to the tissue, followed by the homogenization on ice with slow stokes (approximately 10 strokes). The homogenate was transferred to a fresh centrifuge tube and centrifuged at 1200 x g for 10 min at 4°C and the supernatant was transferred to a fresh tube and centrifuged again at 15,000 x g for 20 min at 4°C. Then, the pellet was resuspended in Syn-PER reagent and Triton X-100 and SDS were added to a final concentration of 1% and 0.1%, respectively, and left at 4°C on a rotating wheel for 1h to lyse synaptosomes and solubilize membrane proteins. The samples were then centrifuged at 16,000 x g for 20 min and the supernatant was used for proteome analysis.  TMT Labelling and High pH reversed-phase chromatography. The TMT analysis of the cell surface proteome samples and the GFP-nanotrap samples has been performed in the same way. i.e. GFP-nanotrap samples were reduced (10mM TCEP, 55°C for 1h), alkylated (18.75mM iodoacetamide, room temperature for 30min.) and then digested from the beads with trypsin (1.25µg trypsin; 37°C, overnight). The resulting peptides were then labeled with TMT ten-plex reagents according to the manufacturer’s protocol (Thermo Fisher Scientific, Loughborough, LE11 5RG, UK) and the labelled samples pooled and desalted using a SepPak cartridge according to the manufacturer’s instructions (Waters, Milford, Massachusetts, USA). Eluate from the SepPak cartridge was evaporated to dryness and resuspended in buffer A (20 mM ammonium hydroxide, pH 10) prior to fractionation by high pH reversed-phase chromatography using an Ultimate 3000 liquid chromatography system (Thermo Scientific).  In brief, the sample was loaded onto an XBridge BEH C18 Column (130Å, 3.5 µm, 2.1 mm X 150 mm, Waters, UK) in buffer A and peptides eluted with an increasing gradient of buffer B (20 mM Ammonium Hydroxide in acetonitrile, pH 10) from 0-95% over 60 minutes. The resulting fractions (concatenated into 5 in total) were evaporated to dryness and resuspended in 1% formic acid prior to analysis by nano-LC MSMS using an Orbitrap Fusion Tribrid mass spectrometer (Thermo Scientific). High pH RP fractions were further fractionated using an Ultimate 3000 nano-LC system in line with an Orbitrap Fusion Tribrid mass spectrometer (Thermo Scientific). In brief, peptides in 1% (vol/vol) formic acid were injected onto an Acclaim PepMap C18 nano-trap column (Thermo Scientific). After washing with 0.5% (vol/vol) acetonitrile 0.1% (vol/vol) formic acid peptides were resolved on a 250 mm × 75 μm Acclaim PepMap C18 reverse phase analytical column (Thermo Scientific) over a 150 min organic gradient, using 7 gradient segments (1-6% solvent B over 1min., 6-15% B over 58min., 15-32%B over 58min., 32-40%B over 5min., 40-90%B over 1min., held at 90%B for 6min and then reduced to 1%B over 1min.) with a flow rate of 300 nl min−1. Solvent A was 0.1% formic acid and Solvent B was aqueous 80% acetonitrile in 0.1% formic acid. Peptides were ionized by nano-electrospray ionization at 2.0kV using a stainless-steel emitter with an internal diameter of 30 μm (Thermo Scientific) and a capillary temperature of 275°C.  All spectra were acquired using an Orbitrap Fusion Tribrid mass spectrometer controlled by Xcalibur 2.1 software (Thermo Scientific) and operated in data-dependent acquisition mode using an SPS-MS3 workflow. FTMS1 spectra were collected at a resolution of 120 000, with an automatic gain control (AGC) target of 200 000 and a max injection time of 50ms. Precursors were filtered with an intensity threshold of 5000, according to charge state (to include charge states 2-7) and with monoisotopic peak determination set to peptide. Previously interrogated precursors were excluded using a dynamic window (60s +/-10ppm). The MS2 precursors were isolated with a quadrupole isolation window of 1.2m/z. ITMS2 spectra were collected with an AGC target of 10 000, max injection time of 70ms and CID collision energy of 35%. For FTMS3 analysis, the Orbitrap was operated at 50 000 resolution with an AGC target of 50 000 and a max injection time of 105ms. Precursors were fragmented by high energy collision dissociation (HCD) at a normalised collision energy of 60% to ensure maximal TMT reporter ion yield. Synchronous Precursor Selection (SPS) was enabled to include up to 10 MS2 fragment ions in the FTMS3 scan."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["MS data analysis. The MS data were searched against the human Uniprot database. Protein groupings were determined by Proteome Discoverer software v2.4 (Thermo Scientific), however, the master protein selection was improved with an in-house script. The script first searches Uniprot for the current status of all protein accessions and updates redirected or obsolete accessions. The script further takes the candidate master proteins for each group, and uses current uniprot review and annotation status to select the best annotated protein as master protein without loss of identification or quantification quality. The protein abundances for each sample were normalised such that all samples had an equal total protein abundance, then normalised abundances were Log2 transformed to bring them closer to a normal distribution. Univariate paired t-tests or linear model analysis were performed for each comparison of interest using normalised abundances. For all comparisons, the p-value was adjusted for multiple testing using the Benjamini-Hochberg method."],"omics_type":["Proteomics"],"labhead":["Peter J. Cullen"],"instrument_platform":[""],"labhead_affiliation":["School of Biochemistry, Faculty of Life Sciences, University of Bristol,UK"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["kohji.kato@bristol.ac.uk"],"publication":["10.1126/SCITRANSLMED.ADT2426"],"submitter_affiliation":["University of Bristol"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Synaptosome analysis Vps35l conditional knock-out mouse","description":"Here, using synaptosome analysis of Vps35l-cKOSynapsin1, we provide a data-rich resource that reveals novel molecular insights into how VPS35L work in 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