{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_proteinGroups.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_peptides.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_parameters.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_Rhot_R1_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_Rhot_R3_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_Rhot_R2_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_GFP_R3_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_GFP_R2_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_Rhot_R4_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_GFP_R4_F4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_GFP_R1_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_GFP_R2_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_GFP_R4_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_Rhot_R2_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_Rhot_R1_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_Rhot_R3_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_Rhot_R4_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_GFP_R3_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD069743/Interaction_GFP_R1_F1.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["Riehle.Christian@mh-hannover.de"],"submitter":["Felix Polten"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Heart","Rhot1","Rhot2","Mouse"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069743"],"tissue":["Heart"],"sample_protocol":["For RHOT1/2 pulldown, HEK-293 cells were co-transfected with His-tagged plasmids encoding human RHOT1 and RHOT2 cDNA sequences using PEI 25K. The His-tagged plasmid encoding green fluorescent protein (GFP) served as control. A premixed solution containing 3 µg of DNA (RHOT1 and RHOT2, 1.5 µg each) and 9 µg of PEI was used for each 10 cm dish containing 1.5 * 10^6 HEK-293 cells, which were cultured for 24h in DMEM supplemented with 10% FBS. Cell lysates were prepared in NP-40 buffer. For immunoprecipitation of RHOT1/2 or GFP, 4 µg of anti His-tag antibody was added to HEK-293 cell lysates and incubated overnight at 4°C. Next, 1.5 mg superparamagnetic beads were added, which was followed by a 30-minute incubation at room temperature. Beads were washed in PBS containing 0.02% Tween-20. To pulldown RHOT1/2 interaction partners, beads-captured RHOT1/2 proteins were incubated with 500 µg of proteins that were isolated from murine left ventricular tissue with NP-40 buffer. Following incubation for 2h at 4°C, RHOT1/2-bound protein complexes were purified by using magnetic beads and washed with PBS containing 0.02% Tween. Samples were washed in pure 10 PBS prior to proteomic analysis. Data were generated from 4 independently prepared samples per condition."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Database search was performed against reviewed mouse entries of Uniprot DB using MaxQuant (version 2.0.1.0). Protein identification was controlled by FDR<0.01 at the protein and peptide level.Mean differences were calculated between transfection with His-tagged plasmids encoding human RHOT1 and RHOT2 cDNA relative to transfection with a His-tagged plasmid encoding GFP. A threshold of log2 fold change >2 was applied to exclude weakly enriched proteins."],"omics_type":["Proteomics"],"labhead":["Christian Riehle"],"instrument_platform":[""],"labhead_affiliation":["Hannover Medical School, Department of Cardiology and Angiology"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["polten.felix@mh-hannover.de"],"publication":["41834725 Froese N, Shymotiuk I, Froese A, Polten F, Jablinski J, Scholz T, Korf-Klingebiel M, Werlein C, Galuppo P, Gigina A, Wihler K, Schneider J, Erschow S, Heimerl M, Szaroszyk M, Hegermann J, Wrede C, Schweitzer T, Pich A, Geffers R, Ricke-Hoch M, Kühnel MP, Jonigk DD, Wende AR, Abel ED, Nikolaev VO, Wollert KC, Bauersachs J, Riehle C. RHOT Proteins Link Mitochondrial Motility to Cardiomyocyte Sarcomere Maturation. Circ Res. 2026 138(9):e327297 10.1161/circresaha.125.327297"],"submitter_affiliation":["Hanover Medical School - Division of Molecular and Translational Cardiology"],"submitter_country":["Germany"],"pubmed_abstract":["<h4>Background</h4>Cardiomyocyte mitochondria align with sarcomeres during heart development. Mitochondrial motility is controlled by RHOT (ras homolog family member T) 1 and RHOT2. RHOT1 and RHOT2 are atypical Rho-like small GTPases that are anchored to the outer mitochondrial membrane and couple mitochondria to kinesin and dynein motors. We hypothesized that RHOT protein expression and mitochondrial motility are required for mitochondrial positioning during cardiomyocyte development.<h4>Methods</h4>We generated mice with cardiomyocyte-selective deletion of <i>Rhot1</i> and <i>Rhot2</i> during embryogenesis (cRhot1/2-KO [constitutive and embryonic cardiomyocyte-selective <i>Rhot1</i>/2 knockout]) or tamoxifen-inducible deletion in the adult heart (iRhot1/2-KO [inducible cardiomyocyte-selective <i>Rhot1/2</i> knockout]) to assess the importance of mitochondrial motility during and after cardiomyocyte maturation. Mitochondrial motility was determined by a motor protein-driven single mitochondria motility assay. Respiratory capacity was measured in isolated mitochondria. Intracellular mitochondrial localization and ATP production in isolated cardiomyocytes were assessed by confocal microscopy and after adenoviral expression of the fluorescence resonance energy transfer-based ATP biosensor ATeam. Cardiac ultrastructure was assessed by electron micrographs; mass spectrometry was used for proteome analysis.<h4>Results</h4>cRhot1/2-KO mice developed fatal cardiomyopathy associated with sarcomere disarray and perinuclear accumulation of mitochondria and ATP production. Mitochondria isolated from cRhot1/2-KO hearts exhibited impaired motility but preserved respiratory capacity. Mechanistically, proteome analysis identified that RHOT proteins bind mitochondria to contractile muscle fiber proteins. In contrast, inducible deletion of <i>Rhot1</i> and <i>Rhot2</i> in adult iRhot1/2-KO mice did not result in heart failure. Despite impaired motility of isolated mitochondria, intracellular mitochondrial localization, local ATP production, and sarcomere structure were preserved in adult iRhot1/2-KO hearts after cardiomyocyte maturation.<h4>Conclusions</h4>RHOT proteins bind mitochondria to contractile muscle fiber proteins and are required for mitochondrial positioning in cardiomyocytes during development. Our study links mitochondrial motility and local ATP production to structural and functional maturation of the heart."],"pubmed_title":["RHOT Proteins Link Mitochondrial Motility to Cardiomyocyte Sarcomere Maturation."],"pubmed_authors":["Froese Natali N, Shymotiuk Ivanna I, Froese Alexander A, Polten Felix F, Jablinski Jonas J, Scholz Tim T, Korf-Klingebiel Mortimer M, Werlein Christopher C, Galuppo Paolo P, Gigina Anna A, Wihler Katharina K, Schneider Johanna J, Erschow Sergej S, Heimerl Maren M, Szaroszyk Malgorzata M, Hegermann Jan J, Wrede Christoph C, Schweitzer Theresa T, Pich Andreas A, Geffers Robert R, Ricke-Hoch Melanie M, Kühnel Mark P MP, Jonigk Danny D DD, Wende Adam R AR, Abel E Dale ED, Nikolaev Viacheslav O VO, Wollert Kai C KC, Bauersachs Johann J, Riehle Christian C"],"additional_accession":[]},"is_claimable":false,"name":"RHOT proteins link mitochondrial motility to cardiomyocyte sarcomere maturation","description":"Proteome analysis of RHOT1/2 interaction partners based on affinity 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