{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077305/FB_AH_late_troph_coIP_proteinGroups.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077305/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077305/FB_AH_CoIP20251_Fmore_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077305/FB_AH_CoIP20251_MyoK_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077305/FB_AH_CoIP20251_F3_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077305/FB_AH_CoIP20251_F2_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077305/FB_AH_CoIP20251_pre_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077305/FB_AH_CoIP20251_F1_2.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["fb207@cam.ac.uk"],"submitter":["Robin Antrobus"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Malaria"],"software":[""],"submitter_keywords":["Malaria","Ip-ms","Trafficking","Myosin"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077305"],"tissue":["Blood Cell","Cell Culture"],"sample_protocol":["All co-immunoprecipitation samples were analysed using suspension trapping (S-Trap) at the Cambridge Institute for Medical Research (CIMR) proteomics core facility. Samples were lysed in 5 % sodium dodecyl sulphate (SDS) in 50 mM triethylammonium bicarbonate (TEAB), reduced in 10 mM dithiothreitol (DTT) at 56 °C for 30 min and akylated with 20 mM iodoacetamide (IAA) at room temperature for 30 min. Proteins were digested overnight at 37oC with Trypsin/Lys-C protease mix (Promega) in 50 mM TEAB at an enzyme to protein ratio of 1: 20 (w/w). Peptides were eluted off the S-Trap column by sequential washes of 40 μl 50 mM TEAB, 40 μl 0.2% formic acid (FA) in water and 40 μl 0.2% FA in 50% acetonitrile.  Eluates were pooled, dried in a SpeedVac and resuspended in MS loading solvent (3% acetonitrile, 0.1% trifluoroacetic acid (TFA)). Peptides were analysed on a Q Exactive Plus mass spectrometer (Thermo Fisher Scientific) coupled to an Ultimate 3000 RSLCnano UPLC system (Thermo Fisher Scientific). Separation was performed on a 50 cm C18 PepMap EASY-Spray column using a gradient from 3% to 40% solvent B over 70 min (solvent A: 0.1% formic acid in water; Solvent B: 80% acetonitrile, 0.1% formic acid). Data were acquired in a Top10 data-dependent acquisition mode.  Full MS spectra were collected over an m/z range of 400-1500 at 70,000 resolution (FWHM) and MSMS spectra were acquired at 17,500 resolution with a dynamic exclusion 30 s."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Raw files were processed as a single batch using the MaxQuant (version 2.6.7.0). Spectra were searched against the reviewed Uniprot Plasmodium falciparum database (downloaded 04/2024)."],"omics_type":["Proteomics"],"labhead":["Folma Buss"],"instrument_platform":[""],"labhead_affiliation":["Cambridge Institute for Medical Research, University of Cambridge; Cambridge, UK"],"submission_type":["PARTIAL"],"species":["Plasmodium (paraplasmodium)"],"publication":["Not available"],"submitter_mail":["pra29@cam.ac.uk"],"submitter_affiliation":["CIMR medicine"],"submitter_country":["United Nations"],"additional_accession":[]},"is_claimable":false,"name":"Plasmodium falciparum PfMyoF with a Rab-like tail domain associates with perinuclear membranes and trafficking proteins","description":"Members of the myosin superfamily are found in all eukaryotes, including Plasmodium falciparum, the parasite that causes the majority of severe malaria. The P. falciparum genome encodes six myosins, but apart from PfMyoA and B, these remain largely uncharacterised. Here, we characterise PfMyoF, a class XXII myosin, using structural prediction, biochemical assays, and imaging. We show that PfMyoF is a plus-end-directed, processive motor with a long neck region with capacity to bind up to six copies of the calmodulin homologue PfCaM. The PfMyoF tail contains predicted WD40 and Rab-like domains that have not been identified in any other eukarytotic myosin class.  Pull-down experiments identify PfMyoF interactions with trafficking proteins, including the vesicle marker PfRab18.  Expansion and immunoelectron microscopy reveal that PfMyoF localises to a perinuclear membrane compartment and transient knockdown in using the glmS ribozyme system impairs growth, potentially indicating an important function during asexual replication. Our findings define PfMyoF as the first myosin with a Rab-like domain and highlight its potential role in membrane trafficking pathways during the pathogenic blood stages of parasite 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