{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/Samples_conditions_files.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/sample_description.sdrf.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4271_11-8-2022_Gaspari_15197_DIA_140min_3ul_RB6.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4277_11-8-2022_Gaspari_15216_RPB-12-5_140min_3ul_RC3.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/Spectronaut_results.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4267_11-7-2022_Gaspari_15195_DIA_140min_3ul_RB4.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4270_11-7-2022_Gaspari_15196_DIA_140min_3ul_RB5.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4278_11-8-2022_Gaspari_15216_RPB-15_140min_3ul_RC4.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4264_11-7-2022_Gaspari_15192_DIA_140min_3ul_RB1.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4276_11-8-2022_Gaspari_15216_RPB-10_140min_3ul_RC2.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4273_11-8-2022_Gaspari_15199_DIA_140min_3ul_RB8.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4265_11-7-2022_Gaspari_15193_DIA_140min_3ul_RB2.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4280_11-8-2022_Gaspari_15216_RPB-50_140min_3ul_RC6.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4275_11-8-2022_Gaspari_15216_RPB-7-5_140min_3ul_RC1.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4266_11-7-2022_Gaspari_15194_DIA_140min_3ul_RB3.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4279_11-8-2022_Gaspari_15216_RPB-20_140min_3ul_RC5.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/4272_11-8-2022_Gaspari_15198_DIA_140min_3ul_RB7.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD064620/20221109_170145_Gaspari_15216_RPB_TIMS.kit"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["sevasti.gaspari@pharma.uzh.ch"],"submitter":["Sevasti Gaspari"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Brain","Mouse","Myelin","Oligodendrocytes","Tmem117"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD064620"],"tissue":["Brain"],"sample_protocol":["Total protein from the same Corpus Callosum samples was isolated from the first column flow-through obtained during the RNA extraction. In brief, the flow-through was mixed with 9-volumes of -20◦C -cold methanol, incubated for 1 hour at -20◦C and then centrifuged at 4000rpm for 10 minutes. Samples were digested following the SP3 method (Huges, et al., 2019) using magnetic Sera-Mag Speedbeads (Cytiva 45152105050250, 50 mg/ml). Briefly, protein extracts (120 ug) precipitated with methanol were resuspended in SP3 buffer (2% SDS, 10mM DTT, 50 mM Tris, pH 7.5) and heated 10 min at 75°C.  Proteins were then alkylated with 32mM (final) iodoacetamide for 45 min at RT in the dark. Beads were added at a ratio 10:1 (w:w) to samples, and proteins were precipitated on beads with ethanol (final concentration: 60 %). After 3 washes with 80% ethanol, beads were digested in 50ul of 100 mM ammonium bicarbonate with 2.4 ug of trypsin (Promega #V5073). After 1h of incubation at 37°C, the same amount of trypsin was added for an additional 1h of incubation. Supernatant were recovered, and acidified with formic acid (0.5% final concentration). To remove traces of SDS, two volumes of isopropanol, 1% TFA were added to the digests, and the samples were desalted on a strong cation exchange (SCX) plate (Oasis MCX; Waters Corp., Milford, MA) by centrifugation. After washing with isopropanol/1%TFA and 2% acetonitrile/0.1% FA, peptides were eluted in 200ul of 80% MeCN, 19% water, 1% (v/v) ammonia, and dried by centrifugal evaporation.  Aliquots (1/8) of samples were pooled and separated into 6 fractions by off-line basic reversed-phase (bRP) using the Pierce High pH Reversed-Phase Peptide Fractionation Kit (Thermo Fisher Scientific). The fractions were collected in 7.5, 10, 12.5, 15, 20 and 50% acetonitrile in 0.1 % triethylamine (~pH 10). Dried bRP fractions were redissolved in 30 ul 2% acetonitrile with 0.5% TFA, and 3 ul were injected for LC-MS/MS analyses. Individual samples were resuspended in 1000ul of 2% acetonitrile,0.1% formic acid and 3 ul were injected.  LC-MS/MS analyses were carried out on a TIMS-TOF Pro (Bruker, Bremen, Germany) mass spectrometer interfaced through a nanospray ion source (“captive spray”) to an Ultimate 3000 RSLCnano HPLC system (Dionex). Peptides were separated on a reversed-phase custom packed 45 cm C18 column (75 μm ID, 100Å, Reprosil Pur 1.9 um particles, Dr. Maisch, Germany) at a flow rate of 250 nl/min with a 2-27% acetonitrile gradient in 93 min followed by a ramp to 45% in 15 min and to 90% in 5 min (total method time: 140 min, all solvents contained 0.1% formic acid). Identical LC gradients were used for DDA and DIA measurements.   For creation of the spectral library, data-dependent acquisitions (DDA) were carried out on the 6 bRP fractions sample pool using a standard TIMS PASEF method (Meier, et al. 2018) with ion accumulation for 100 ms for each survey MS1 scan and the TIMS-coupled MS2 scans. Duty cycle was kept at 100%. Up to 10 precursors were targeted per TIMS scan. Precursor isolation was done with a 2 Th or 3 Th windows below or above m/z 800, respectively. The minimum threshold intensity for precursor selection was 2500.  If the inclusion list allowed it, precursors were targeted more than one time to reach a minimum target total intensity of 20’000. Collision energy was ramped linearly based uniquely on the 1/k0 values from 20 (at 1/k0=0.6) to 59 eV (at 1/k0=1.6). Total duration of a scan cycle including one survey and 10 MS2 TIMS scans was 1.16 s. Precursors could be targeted again in subsequent cycles if their signal increased by a factor 4.0 or more.  After selection in one cycle, precursors were excluded from further selection for 60s. Mass resolution in all MS measurements was approximately 35’000.  The data-independent acquisition (DIA) used mostly the same instrument parameters as the DDA method and was as reported previously (Meier, et al. 2020). Per cycle, the mass range 400-1200 m/z was covered by a total of 32 windows, each 25 Th wide and a 1/k0 range of 0.3. Collision energy and resolution settings were the same as in the DDA method. Two windows were acquired per TIMS scan (100ms) so that the total cycle time was 1.7 s."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw Bruker MS data were processed directly with Spectronaut 16.3 (Biognosys, Schlieren, Switzerland). A library was constructed from the DDA bRP fraction data by searching the UNIPROT-SWISSPROT mouse proteome (www.uniprot.org) database of January  7th, 2022 and a contaminant database containing the most usual environmental contaminants and enzymes used for digestion (from Frankenfield, et al., 2022). For identification, peptides of 7-52 AA length were considered, cleaved with trypsin/P specificity and a maximum of 2 missed cleavages. Carbamidomethylation of cysteine (fixed), methionine oxidation and N-terminal protein acetylation (variable) were the modifications applied. Mass calibration was dynamic and based on a first database search. The Pulsar engine was used for peptide identification. Protein inference was performed with the IDPicker algorithm. Spectra, peptide and protein identifications were all filtered at 1% FDR against a decoy database.  Specific filtering for library construction removed fragments corresponding to less than 3 AA and fragments outside the 300-1800 m/z range. Also, only fragments with a minimum base peak intensity of 5% were kept.  Precursors with less than 3 fragments were also eliminated and only the best 6 fragments were kept per precursor. No filtering was done on the basis of charge state and a maximum of 2 missed cleavages was allowed. Shared (non proteotypic) peptides were kept. Peptide-centric analysis of DIA data was done with Spectronaut 15.7 using the library described above. Single hits proteins (defined as matched by one stripped sequence only) were kept in the Spectronaut analysis. Peptide quantitation was based on XIC area, for which a minimum of 1 and a maximum of 3 (the 3 best) precursors were considered for each peptide, from which the median value was selected.  Quantities for protein groups were derived from inter-run peptide ratios based on MaxLFQ algorithm (Cox et al 2014). Global normalization of runs/samples was done based on the median of peptides.  Overall 97’900 peptide precursor ions were quantified in the dataset, mapped to 7’131 protein groups. 83’014 precursors (6’666 protein groups) had full profiles, i.e. were quantified in all samples. The average number of data points per LC peak was 6.2."],"omics_type":["Proteomics"],"labhead":["Sevasti Gaspari"],"instrument_platform":[""],"labhead_affiliation":["Institute of Pharmacology and Toxicology, University of Zurich, CH-8057 Zurich, Switzerland."],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["sevasti.gaspari@pharma.uzh.ch"],"publication":["Not available"],"submitter_affiliation":["Institute of Pharmacology and Toxicology, University of Zurich"],"submitter_country":["Switzerland"],"additional_accession":[]},"is_claimable":false,"name":"Tmem117, an oligodendrocyte-enriched regulator of NCX activity, links central nervous system myelin homeostasis to counterregulation and metabolic health.","description":"The influence of metabolic dysfunction on myelin has been well documented, yet whether central nervous system myelin homeostasis contributes to systemic metabolic regulation remains unclear. Here we identify Tmem117, a previously uncharacterized oligodendrocyte-enriched protein, as a critical regulator of this axis. Conditional deletion of Tmem117 in mature oligodendrocytes induces ER stress, broad proteome dysregulation, and demyelination, with myelin disruption leading to sex-specific effects on counterregulatory response, glucose tolerance, and hepatic lipid accumulation. Mechanistically, we provide evidence that Tmem117 modulates the sodium-calcium exchanger NCX1. These findings uncover a reciprocal link between central nervous system myelin integrity and systemic metabolic homeostasis, and position Tmem117 as a potential target for cell-specific modulation of NCX 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