{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC121M1015A08_report.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/samples_MS.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-A03-P12143-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-B02-P12150-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-A04-P12144-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-B01-P12149-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-A01-P12141-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-C01-P12157-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-B08-P12156-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-A02-P12142-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-B07-P12155-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-A07-P12147-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-B06-P12154-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-A08-P12148-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-C02-P12158-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-B05-P12153-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-A05-P12145-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-B04-P12152-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-A06-P12146-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055357/EC_121-M1015-B03-P12151-1.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["sara.sdelci@crg.eu"],"submitter":["Savvas Kourtis"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":["Not available"],"submitter_keywords":["Enzymes","Chromatin","Cell cycle","Metabolism"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD055357"],"sample_protocol":["Liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) The protein concentrations from chromatin enriched samples were determined using the BCA protein assay kit (Applichem CmBH, Darmstadt,Germany), and 10 μg per sample was processed using an adapted Single-Pot solid-phase-enhanced sample preparation (SP3) methodology (1). Briefly, equal volumes (125 μl containing 6250 µg) of two different kind of paramagnetic carboxylate modified particles (SpeedBeads 45152105050250 and 65152105050250; GE Healthcare) were mixed, washed three times with 250 µl water and reconstituted to a final concentration of 50 μg/μl with LC-MS grade water (LiChrosolv; MERCK KgaA). Samples were filled up to 100 µL with stock solutions to reach a final concentration of 2% SDS, 100mM HEPES, pH 8.0, and proteins were reduced by incubation with a final concentration of 10 mM DTT for 1 hour at 56°C. After cooling down to room temperature, reduced cysteines were alkylated with iodoacetamide at a final concentration of 55 mM for 30 min in the dark. For tryptic digestion, 400 μg of mixed beads were added to reduced and alkylated samples, vortexed gently and incubated for 5 minutes at room temperature. The formed particles-protein complexes were precipitated by addition of acetonitrile to a final concentration of 70% [V/V], mixed briefly via pipetting before incubating for 18 minutes at room temperature. Particles were then immobilized using a magnetic rack (DynaMag-2 Magnet; Thermo Fisher Scientific) and supernatant was discarded. SDS was removed by washing two times with 200 μl 70% ethanol and one time with 180 μl 100% acetonitrile. After removal of organic solvent, particles were resuspended in 100 μl of 50 mM NH4HCO3 and samples digested by incubating with 1 μg of Trypsin overnight at 37°C. Samples were acidified to a final concentration of 1% Trifluoroacetic acid (Uvasol; MERCK KgaA) prior to immobilizing the beads on the magnetic rack. Peptides were desalted using C18 solid phase extraction spin columns (Pierce Biotechnology, Rockford, IL). Finally, eluates were dried in a vacuum concentrator and reconstituted in 10 µl of 0.1% TFA.  Mass spectrometry was performed on an Orbitrap Fusion Lumos mass spectrometer (ThermoFisher Scientific, San Jose, CA) coupled to an Dionex Ultimate 3000RSLC nano system (ThermoFisher Scientific, San Jose, CA) via nanoflex source interface. Tryptic peptides were loaded onto a trap column (Pepmap 100 5μm, 5 × 0.3 mm, ThermoFisher Scientific, San Jose, CA) at a flow rate of 10 μL/min using 0.1% TFA as loading buffer. After loading, the trap column was switched in-line with a 50 cm, 75 µm inner diameter analytical column (packed in-house with ReproSil-Pur 120 C18-AQ, 3 μm, Dr. Maisch, Ammerbuch-Entringen, Germany). Mobile-phase A consisted of 0.4% formic acid in water and mobile-phase B of 0.4% formic acid in a mix of 90% acetonitrile and 10% water. The flow rate was set to 230 nL/min and a 90 min gradient used (4 to 24% solvent B within 82 min, 24 to 36% solvent B within 8 min and, 36 to 100% solvent B within 1 min, 100% solvent B for 6 min before bringing back solvent B at 4% within 1 min and equilibrating for 18 min).  Analysis was performed in a data-independent acquisition (DIA) mode. Full MS scans were acquired with a mass range of 375 - 1250 m/z in the orbitrap, an RF lens set at 40%, and at a resolution of 120,000 (at 200 m/z). The automatic gain control (AGC) was set to a target of 4 × 105, and a maximum injection time of 54 ms was applied, scanning data in profile mode. MS1 scans were followed by 41 MS2 customed windows. The MS2 scans were acquired in the Orbitrap at a resolution of 30,000 (at 200 m/z), with an AGC set to target 2 × 105, for a maximum injection time of 54 ms. Fragmentation was achieved with higher energy collision induced dissociation (HCD) at a fixed normalized collision energy (NCE) of 35%. A single lock mass at m/z 445.120024 (2) was employed. Xcalibur version 4.3.73.11 and Tune 3.4.3072.18 were used to operate the instrument."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data were analysed using the DIANN software with default conditions"],"omics_type":["Proteomics"],"labhead":["Sara Sdelci"],"instrument_platform":[""],"labhead_affiliation":["Center for genomic regulation Barcelona"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["kourtissavvas@gmail.com"],"publication":["42011901 Gañez-Zapater A, Kourtis S, Elbæk CR, Espinar L, Toro-Márquez C, Coll-Manzano A, Smiriglia A, García-López L, Wiegand L, Guirola M, Fontaine F, Morandi A, Müller AC, Sdelci S. Cell Cycle Control of Nuclear Metabolism Couples Phosphatidylinositol Signaling to Histone Methylation. Adv Sci (Weinh). 2026 13(34):e01083 10.1002/advs.202501083"],"submitter_affiliation":["CRG"],"submitter_country":["Spain"],"pubmed_abstract":["Progression through the cell cycle requires coordinated regulation of transcription, chromatin state, and cellular metabolism. While metabolic enzymes are known to localize the nucleus and influence chromatin states, how nuclear metabolism itself oscillates during the cell cycle remains unexplored. Here, we combine a customized FUCCI-3 reporter with chromatome mass spectrometry and high-throughput imaging to systematically resolve nuclear and chromatin-associated metabolic changes across cell cycle phases. We identify phosphatidylinositol metabolism as a nuclear pathway that oscillates with the cell cycle, with PIP5K1A, PLCD3, and PLD2 showing phase-specific nuclear and chromatin dynamics. Nuclear PIP2 levels redistribute within the nucleus depending on cell cycle stage. Downregulation of PIP5K1A reduces nuclear PIP2 levels, whereas nuclear enrichment of PIP5K1A increases PIP2 abundance in the nucleus and nucleolus, functionally linking PIP5K1A nuclear localization to nuclear PIP2 synthesis. Moreover, perturbation of nuclear PIP2 synthesis alters chromatin methylation, with a pronounced impact on H4K20 monomethylation. Together, our results reveal that nuclear phosphatidylinositol metabolism is cell cycle regulated and functionally linked to chromatin methylation, establishing nuclear lipid metabolism as a previously unrecognized layer of cell cycle control."],"pubmed_title":["Cell Cycle Control of Nuclear Metabolism Couples Phosphatidylinositol Signaling to Histone Methylation."],"pubmed_authors":["Gañez-Zapater Antoni A, Kourtis Savvas S, Elbæk Camilla Reiter CR, Espinar Lorena L, Toro-Márquez Carolina C, Coll-Manzano Albert A, Smiriglia Alfredo A, García-López Laura L, Wiegand Laura L, Guirola Maria M, Fontaine Frédéric F, Morandi Andrea A, Müller André C AC, Sdelci Sara S"],"additional_accession":[]},"is_claimable":false,"name":"Chromatin cell cycle proteomics reveals nuclear metabolism","description":"The progression of the cell cycle is regulated by the expression of specific genes and fluctuations in cellular metabolic states. By conducting cell cycle-based transcriptomics, proteomics, and metabolomics analyses, previous research has identified cell cycle-dependent alterations at the molecular, protein, and metabolic levels.  However, the significance of protein compartmentalization, coupled with the evidence that metabolic enzymes can localize to the nucleus and influence chromatin states, suggests that fluctuations in nuclear metabolism may play a role in regulating cell cycle progression. In this study, we present a systematic approach to investigating the chromatin environment at a cell cycle resolution. By focusing on metabolic enzymes, we were able to ascertain that phosphatidylinositol metabolism localizes to the nucleus and undergoes alterations throughout the cell cycle. Moreover, the inhibition of phosphatidylinositol metabolism affects histone methylation in a manner that is dependent on the cell cycle, which ultimately impairs cell cycle progression. Our study demonstrates that nuclear metabolism is a dynamic process that shapes the chromatin environment and establishes a direct connection between nuclear metabolism and the cell 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