{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070965/checksum.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070965/pl24071_RYanase_FT.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070965/pl24071_RYanase_P.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070965/20241121_LU50HMC10_pl24071_RY_FT.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070965/20241121_LU50HMC08_pl24071_RY_phospho.raw"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070965/pl24071_RYanase_FT.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070965/pl24071_RYanase_P.mzid"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["rita.tewari@nottingham.ac.uk"],"submitter":["Ryuji Yanase"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Malaria"],"software":[""],"submitter_keywords":["Plasmodium berghei","Nek4","Phosphoproteomics","Zygote","Meiosis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070965"],"tissue":["Zygote"],"sample_protocol":["Protein Extraction and Digestion via SDS-FASP: Plasmodium Zzygotes of WT and Pbnek4-ko lines at 0 and 2 hpa were lysed in 300  μl 400  μl of buffer containing 2% SDS, 25  mM NaCl, 50  mM Tris-HCl (pH 7.4), 2.5  mM EDTA, and 20  mM TCEP, supplemented with a protease and phosphatase inhibitor cocktail (Halt, Thermo Fisher Scientific). Samples were vortexed and heated at 95°C for 10 min with continuous mixing at 40 0 rpm. Genomic DNA was fragmented using four 10-second sonication pulses at 50% amplitude. Following centrifugation at 17,000 g for 30 min, supernatants were collected, and protein concentrations were determined using the Pierce BCA 660nm Protein Assay Kit. For alkylation the volume corresponding to 1 mg of protein for each sample was adjusted to in,  300  μl of each sample was and then incubated with 48  μl of 0.5  M iodoacetamide for 1 h at room temperature in the dark. Protein digestion was performed using the filter-aided sample preparation (FASP) method with Amicon Ultra-4 30  kDa centrifugal filter units (Millipore). Trypsin (Promega) was added at a 1:80 enzyme-to-protein ratio, and digestion proceeded overnight at room temperature. Resulting peptides were desalted using Pierce Peptide Desalting Spin Columns (Thermo Fisher Scientific) according to the manufacturer's instructions and dried using a speed vacuum concentrator. TMT-11plex Labelling: Peptide concentrations were measured using the Pierce Quantitative Colorimetric Peptide Assay (Thermo Fisher Scientific). For each sample, 100  μg 160  μg of peptides were labelled with 400  μg 800  μg of TMTpro reagents (Thermo Fisher Scientific), previously dissolved in 11 0 μl 220  μl of 36% acetonitrile and 200  mM EPPS buffer (pH 8.5). Labelling reactions were carried out for 1 h at room temperature and quenched by adding hydroxylamine to a final concentration of 0.3% (v/v). Labelled samples were pooled, desalted using Pierce Peptide Desalting Spin Columns, and dried under vacuum. Phosphopeptide Enrichment: Phosphopeptides were enriched using the High-Select Fe-NTA Phosphopeptide Enrichment Kit (Thermo Fisher Scientific) following the manufacturer's protocol. Both the enriched phosphopeptide fractions and the flow-through were desalted using Pierce Peptide Desalting Spin Columns and dried using a speed vacuum concentrator. LC-MS/MS Analysis: Dried peptides were reconstituted in 5% acetonitrile with 0.1% formic acid, and 2  μg of each sample was injected into a Vanquish NEO liquid chromatography system (Thermo Fisher Scientific)an Easy-nLC 1200 system coupled to an Orbitrap Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific). Peptides were first trapped on an Acclaim PepMap 100 C18 trap column (75 μm × 20 mm, 3 μm particle size) and then separated on a homemade analytical column (75  μm × 500  mm) packed with ReproSil-Pur C18 resin (1.9  μm, 100 Å, Dr. Maisch GmbH). The analytical separation was run for 180 min using a gradient of H2O/FA 99.9%/0.1% (solvent A) and CH3CN/H2O/FA 80.0%/19.9%/0.1% (solvent B). The gradient was run from 5 % B to 28 % B in 160 min, then to 40% B in 20 min, then to 99% B in 10 min with a final stay of 20 min at 99 % B. Flow rate was of 250 nL/min an total run time was of 210 min.The gradient elution was performed over 180 min at a flow rate of 250 nL/min, starting from 8% to 28% solvent B (80% acetonitrile, 0.1% formic acid) over 160 min, then to 40% B over 20 min, and finally to 95% B over 10 min, holding at 95% B for an additional 20 min. The mass spectrometer was operated in data-dependent acquisition mode. Full MS scans were acquired in the Orbitrap at a resolution of 120,000 (at m/z 200), with an AGC target of 4 × 105 and a maximum injection time of 50 ms. MS/MS scans were performed in the Orbitrap at a resolution of 50,000, with an AGC target of 5 × 104, a maximum injection time of 86 ms, and a normalized collision energy of 33% using higher-energy collisional dissociation (HCD). The isolation window was set to 0.7 m/z, and dynamic exclusion was enabled with a duration of 60 seconds. Data-Dependent Acquisition (DDA) was performed with MS1 full scan at a resolution of 120’’000 FWHM followed by as many subsequent MS2 scans on selected precursors as possible within 3 second maximum cycle time. MS1 was performed in the Orbitrap with an AGC target of 4x105, a maximum injection time of 50 ms and a scan range from 375 to 1500 m/z. MS2 was performed in the Orbitrap at a resolution of 50’000 FWHM using higher-energy collisional dissociation HCD at 38% NCE. Isolation windows was at 0.7 u with an AGC target of 5x104 and a maximum injection time of 86 ms. A dynamic exclusion of parent ions of 60 s. with 10 ppm mass tolerance was applied."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw data files were processed using Proteome Discoverer software version 2.4 (Thermo Fisher Scientific). Spectra were searched against the P. berghei ANKA protein database (PlasmoDB.org release 68), the mus musculus reference proteome database (UniProt, reviewed, release 2024_06, 17’207 entries) and an in-house database of common contaminants using the Mascot search engine (version 2.6.2, Matrix Science). Search parameters included trypsin as the digestion enzyme with up to one missed cleavage allowed, a precursor mass tolerance of 10 ppm, and a fragment mass tolerance of 0.02 Da. Carbamidomethylation of cysteine (+57.021 Da) and TMT modification of peptide N-termini and lysine residues (+229.163 Da) were set as fixed modifications, while oxidation of methionine (+15.995 Da) and phosphorylation of serine, threonine, and tyrosine (+79.966 Da) were set as variable modifications. Peptide-spectrum matches (PSMs) and peptides were validated using the Percolator algorithm, applying a false discovery rate (FDR) of 1%. Proteins were inferred from the identified peptides and filtered to achieve an FDR of 1%. Quantitative information was extracted using reporter ion intensities from TMT tags, and protein abundances were normalized based on the total peptide amount and scaled across all samples. Protein ratios were calculated using the summed abundances-based approach across groups, and statistical significance was assessed using ANOVA."],"omics_type":["Proteomics"],"labhead":["Rita Tewari"],"instrument_platform":[""],"labhead_affiliation":["School of Life Science, Queen's Medical Centre, University of Nottingham"],"submission_type":["COMPLETE"],"species":["Plasmodium Berghei Anka"],"publication":["41510253 Yanase R, Hair M, Zeeshan M, Ferguson DJP, Brady D, Pasquarello C, Bottrill A, Bhanvadia S, Neal A, Tromer EC, Le Roch KG, Hainard A, Holder AA, Vaughan S, Guttery DS, Tewari R. A divergent &lt;i&gt;Plasmodium&lt;/i&gt; NEK4 acts as a key regulator driving the early events of meiosis. Res Sq. 2025:rs.3.rs-8180258 10.21203/rs.3.rs-8180258/v1"],"submitter_mail":["ryuji.yanase@gmail.com"],"submitter_affiliation":["University of Nottingham"],"submitter_country":["United Kingdom"],"doi":["10.6019/PXD070965"],"pubmed_abstract":["Meiosis is a conserved yet evolutionarily varied process underpinning sexual reproduction in eukaryotes. In the malaria parasite <i>Plasmodium</i>, meiosis is unconventional: it occurs immediately after fertilisation (post-zygotic) and must be coordinated with the transformation of the zygote into a motile ookinete. The mechanisms synchronising these meiotic and morphogenetic programmes remain unknow. Here, we identify the <i>Plasmodium berghei</i> NIMA-related kinase, NEK4 as a key regulator that couples meiotic initiation with zygote morphogenesis. Using ultrastructure expansion microscopy, we show that NEK4 accumulates at the microtubule-organising centre (MTOC) and the apical polar complex (APC) shortly after fertilisation, preceding the assembly of perinuclear and cortical microtubules. We reveal that <i>Plasmodium</i> zygotes undergo a nuclear migration driven by the MTOC, analogous to the meiotic nuclear movement in fission yeast. Deletion of <i>nek4</i> results in complete developmental arrest: MTOC duplication and microtubule formation are blocked, chromatin remains uncondensed, and nuclear migration and cell polarity fail to establish. Transcriptomic and phosphoproteomic analyses reveal that NEK4 absence causes a collapse in transcriptional and phosphoregulatory networks governing meiosis and cytoskeletal organisation, leading to reduced expression and phosphorylation of important players, including HOP1, REC8, and AP2-O. These findings establish NEK4 as a key regulator driving meiotic entry and zygote maturation."],"pubmed_title":["A divergent &lt;i&gt;Plasmodium&lt;/i&gt; NEK4 acts as a key regulator driving the early events of meiosis."],"pubmed_authors":["Yanase Ryuji R, Hair Molly M, Zeeshan Mohammad M, Ferguson David J P DJP, Brady Declan D, Pasquarello Carla C, Bottrill Andrew A, Bhanvadia Suhani S, Neal Arrmund A, Tromer Eelco C EC, Le Roch Karine G KG, Hainard Alexandre A, Holder Anthony A AA, Vaughan Sue S, Guttery David S DS, Tewari Rita R"],"additional_accession":[]},"is_claimable":false,"name":"Plasmodium berghei zygotes of WT and Pbnek4-ko lines at 0 and 2 hpa phosphoproteomics","description":"Meiosis is a conserved yet evolutionarily varied process that underpins sexual reproduction in eukaryotes. In the malaria parasite Plasmodium, meiosis occurs within the mosquito midgut immediately after fertilisation, as the diploid zygote differentiates into a motile ookinete. Here, we identify the Plasmodium berghei NIMA-related kinase, NEK4 as a key regulator that coordinates meiotic initiation with zygote morphogenesis. Meiosis in Plasmodium spp. is highly divergent from that of most canonical models, since many conserved meiotic regulators are absent, and employs lineage-specific adaptations of protein function. Using gene tagging and ultrastructure expansion microscopy, we show that NEK4 is located at the microtubule-organising centre (MTOC) and the apical polar complex (APC) during early zygote development. NEK4-GFP foci appear shortly after fertilisation, followed by perinuclear and cortical microtubule formation. Deletion of nek4 results in complete developmental arrest: MTOC duplication and DNA replication are blocked, chromatin remains uncondensed, and nuclear migration and cell polarity fail to establish. Transcriptomic and phosphoproteomic analyses revealed that absence of NEK4 causes a collapse in transcriptional and phosphoregulatory networks controlling meiosis and cytoskeletal organisation. nek4 gene knockout parasites had reduced expression of genes linked to meiotic division, motility, and differentiation, and reduced phosphorylation of important players such as DMC1, AP2-Z, Pb103, HOP1, and REC8 proteins. These findings establish NEK4 as a key regulator governing transcriptional activation, protein synthesis, and phosphoregulation to drive meiotic entry and zygote 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