{"gene":"TOMM7","run_date":"2026-04-28T21:42:59","timeline":{"discoveries":[{"year":1996,"finding":"Tom7 is a small integral membrane subunit of the mitochondrial outer membrane translocase (TOM complex) that destabilizes the interaction between receptors Tom20 and Tom22 and the import pore component Tom40, while Tom6 stabilizes this interaction; deletion of Tom7 inhibits import of outer membrane protein porin and delays two-step import of matrix-destined preproteins, and genetic synthetic lethality of tom7Δ tom20Δ and tom7Δ tom6Δ double mutants confirms functional relationships.","method":"Genetic deletion, in vitro import assays, native protein complex analysis, double-mutant synthetic growth defect analysis","journal":"The EMBO journal","confidence":"High","confidence_rationale":"Tier 2 — multiple orthogonal methods (genetic, biochemical import assays, complex assembly), foundational study replicated by subsequent work","pmids":["8641278"],"is_preprint":false},{"year":2001,"finding":"Tom7 in Neurospora crassa is in direct physical contact with the major pore component Tom40, as shown by cross-linking, and its precursor can insert into the outer membrane in vitro and assemble into authentic TOM complexes via a pathway that shares a binding site with the general import pathway and depends on receptor components.","method":"Cross-linking, in vitro import and assembly assays, competition assays","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1–2 — in vitro reconstitution of assembly with cross-linking confirming direct Tom40 contact","pmids":["11278536"],"is_preprint":false},{"year":2002,"finding":"Human Tom7 is a tail-anchored protein imported into mitochondria in a nucleotide-independent manner, anchored to the outer membrane with its C terminus facing the intermembrane space; it assembles first into an ~120 kDa intermediate containing Tom40 but lacking receptors, then into the ~380 kDa TOM complex additionally containing Tom22; Tom22 is rate-limiting for this final assembly step.","method":"In vitro import into HeLa mitochondria, blue native electrophoresis, supershift antibody analysis, Tom22 overexpression","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 — multiple orthogonal biochemical methods in human cells with functional overexpression validation","pmids":["12198123"],"is_preprint":false},{"year":2002,"finding":"Tom7 is a tail-anchored protein whose carboxy-terminal 33 amino acids contain mitochondrial outer membrane targeting information, and a conserved proline residue within the transmembrane segment is required for efficient targeting to the outer membrane.","method":"Deletion/truncation mutagenesis, proline point mutation, subcellular targeting assays","journal":"FEBS letters","confidence":"Medium","confidence_rationale":"Tier 2 — mutagenesis with targeting readout, single lab","pmids":["11943179"],"is_preprint":false},{"year":2006,"finding":"Tom7 promotes segregation of the SAM complex subunit Mdm10 into a low-molecular-mass form away from the SAM(holo) complex; deletion of Tom7 increases the fraction of Mdm10 in the SAM(holo) complex, explaining the opposing roles of Tom7 (promotes porin assembly, antagonizes Tom40 assembly) versus Mdm10 (promotes Tom40 assembly).","method":"Genetic deletion, co-immunoprecipitation, native gel electrophoresis, in vitro import/assembly assays","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 — genetic and biochemical orthogonal methods with clear epistatic placement of Tom7 relative to Mdm10 and SAM complex","pmids":["16760475"],"is_preprint":false},{"year":2010,"finding":"Tom7 directly interacts with Tom40 through its transmembrane segment and with Mdm10, as shown by site-specific photocross-linking in vivo; Tom7 recruits Mdm10 to enhance its association with the MMM1 complex and regulates the timing of Tom40 release from the TOB/SAM complex for subsequent assembly into the TOM40 complex.","method":"Site-specific photocross-linking in vivo, in vitro import assays, Tom7 overexpression/depletion","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1–2 — in vivo site-specific cross-linking directly demonstrating protein contacts, complemented by functional import assays","pmids":["21036907"],"is_preprint":false},{"year":2010,"finding":"Tom7 plays inhibitory roles at two distinct steps in TOM complex biogenesis: (1) antagonizing Tom5 and Tom6 at an early stage of Tom40 assembly at the SAM complex, and (2) interacting with Mdm10 not bound to the SAM complex to promote dissociation of the SAM-Mdm10 complex, thereby delaying assembly of Tom22 with Tom40 at a late stage.","method":"Genetic deletion, native gel electrophoresis, in vitro import assays, complex assembly tracking","journal":"Journal of molecular biology","confidence":"High","confidence_rationale":"Tier 2 — multiple orthogonal biochemical steps dissected, consistent with and extending prior studies","pmids":["21059357"],"is_preprint":false},{"year":2019,"finding":"Tom7 is required for PINK1 import arrest at the outer mitochondrial membrane upon mitochondrial depolarization; deletion of Tom7 causes PINK1 to be imported into depolarized mitochondria and cleaved by the OMA1 protease rather than accumulating at the outer membrane. A negatively charged amino acid cluster motif just C-terminal to the PINK1 transmembrane domain mediates this retention, and Tom7 and OMA1 act in a 'tug of war' to determine PINK1 fate.","method":"Tom7 deletion, OMA1 suppression, mutagenesis of PINK1 motif, PINK1 localization and cleavage assays","journal":"Molecular cell","confidence":"High","confidence_rationale":"Tier 2 — genetic and biochemical epistasis with mutagenesis, highly cited foundational study replicated across multiple conditions","pmids":["30733118"],"is_preprint":false},{"year":2018,"finding":"Tomm7 in endothelial cells controls cerebrovascular network formation by regulating the mitochondrial import of Rac1; Tomm7 deficiency causes increased import of Rac1 into mitochondria, activating mitochondrial Rac1-coupled redox signaling that impairs angiogenesis and underlies cerebrovascular malformation.","method":"Zebrafish loss-of-function genetic screen, Tomm7 knockout mice, endothelial-specific transgenic rescue, mitochondrial import assays, vascular imaging","journal":"Arteriosclerosis, thrombosis, and vascular biology","confidence":"Medium","confidence_rationale":"Tier 2 — multiple model organisms and genetic rescue, but mechanistic link to Rac1 import based on single lab","pmids":["30354240"],"is_preprint":false},{"year":2022,"finding":"A homozygous missense variant (p.Pro29Leu) in human TOMM7 causes a progeroid syndrome with severe growth retardation; proband-derived fibroblasts show altered mitochondrial protein import with increased abundance of oxidative phosphorylation proteins and reduced phospholipid metabolism proteins, and elevated basal and maximal oxygen consumption rates.","method":"Exome sequencing, quantitative mitochondrial proteomics, oxygen consumption rate measurement in patient fibroblasts","journal":"The Journal of clinical investigation","confidence":"Medium","confidence_rationale":"Tier 2 — patient variant with proteomics and functional metabolic readout, single family report","pmids":["36282599"],"is_preprint":false},{"year":2022,"finding":"A homozygous hypomorphic variant in TOMM7 (p.Trp25Arg) causes syndromic short stature and developmental delay; Tomm7 mutant mice show mitochondrial uncoupling with increased oxygen consumption but normal ETC function, suggesting Tomm7 deficiency uncouples oxidation from ATP synthesis without impairing TCA cycle or ETC.","method":"Mouse knockout and knock-in models, oxygen consumption assays with ETC inhibitors, phenotypic characterization","journal":"HGG advances","confidence":"Medium","confidence_rationale":"Tier 2 — mouse models with functional mitochondrial assays, single lab","pmids":["36299998"],"is_preprint":false},{"year":2025,"finding":"TOMM7 regulates PINK1/Parkin-mediated mitophagy in kidney tubular cells by modulating the intracellular redistribution of phospholipase PLA2G6 between the nucleus and mitochondria; TOMM7 overexpression in db/db mice restores PINK1/Parkin-mediated mitophagy and alleviates tubular injury. ZBTB12 was identified as a transcriptional repressor of TOMM7.","method":"Tomm7 overexpression in db/db mice, PLA2G6 localization assays, ZBTB12 transcription factor identification, tubular cell in vitro models","journal":"Kidney international","confidence":"Medium","confidence_rationale":"Tier 2 — in vivo overexpression with mechanistic follow-up on PLA2G6 redistribution, single lab","pmids":["41276015"],"is_preprint":false},{"year":2025,"finding":"CRISPR knockout of TOM7 in human iPSC-derived dopaminergic neurons decreases ubiquitin pSer65 upregulation during mitophagy activation, confirming Tom7's role in the PINK1-PARKIN mitophagy pathway in a human neuronal model.","method":"High-throughput arrayed CRISPR-Cas9 screen, high-content immunofluorescence imaging, machine learning analysis in iPSC-derived dopaminergic neurons","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 2 — functional genomic screen in disease-relevant human neuronal model, preprint","pmids":["bio_10.1101_2025.06.10.658840"],"is_preprint":true}],"current_model":"TOMM7 encodes a small tail-anchored integral membrane subunit of the mitochondrial outer membrane TOM translocase complex that directly contacts Tom40 via its transmembrane segment, destabilizes TOM complex assembly by antagonizing Tom5/Tom6 and by segregating Mdm10 from the SAM-Mdm10 complex, is specifically required for PINK1 import arrest on depolarized mitochondria (opposing OMA1-mediated PINK1 cleavage in a regulated 'tug of war'), and regulates PINK1/Parkin-dependent mitophagy as well as selective import of substrates such as Rac1 and PLA2G6, thereby controlling mitochondrial homeostasis, angiogenesis, and cellular responses to damage."},"narrative":{"teleology":[{"year":1996,"claim":"Identification of Tom7 as a small TOM complex subunit with a destabilizing role in receptor–pore interactions established that TOM assembly is actively modulated rather than merely driven by affinity, and that Tom7 opposes Tom6 function.","evidence":"Yeast gene deletion with in vitro import assays, native complex analysis, and synthetic lethality (tom7Δ tom20Δ, tom7Δ tom6Δ)","pmids":["8641278"],"confidence":"High","gaps":["Direct physical contacts between Tom7 and other TOM subunits not yet mapped","Mechanism of how Tom7 destabilizes receptor–pore interaction unknown"]},{"year":2001,"claim":"Cross-linking experiments resolved that Tom7 makes direct physical contact with Tom40 through its transmembrane domain, establishing that Tom7 acts on the pore itself rather than indirectly through receptors.","evidence":"Chemical cross-linking and in vitro assembly/competition assays in Neurospora crassa mitochondria","pmids":["11278536"],"confidence":"High","gaps":["Residue-level contacts not defined","Whether human Tom7 contacts Tom40 identically was unconfirmed"]},{"year":2002,"claim":"Characterization of human Tom7 as a tail-anchored protein that assembles stepwise into TOM complexes via a ~120 kDa Tom40-containing intermediate before joining the ~380 kDa holo-complex established the assembly pathway in mammalian cells and identified Tom22 as rate-limiting for the final step.","evidence":"In vitro import into HeLa mitochondria, blue native PAGE, antibody supershift, Tom22 overexpression","pmids":["12198123","11943179"],"confidence":"High","gaps":["Functional consequences of Tom7 loss in human cells not yet tested","Role of the conserved transmembrane proline in assembly kinetics not fully resolved"]},{"year":2006,"claim":"Discovery that Tom7 promotes segregation of Mdm10 away from the SAM(holo) complex explained its paradoxical dual role — promoting porin assembly while antagonizing Tom40 assembly — by placing Tom7 as a regulator of SAM complex composition.","evidence":"Yeast genetic deletion, co-immunoprecipitation, native gel electrophoresis, in vitro import/assembly","pmids":["16760475"],"confidence":"High","gaps":["Direct Tom7–Mdm10 interaction not yet proven by cross-linking","Whether Mdm10 regulation is conserved in mammals unknown"]},{"year":2010,"claim":"In vivo site-specific photocross-linking confirmed that Tom7 contacts both Tom40 (via its transmembrane segment) and Mdm10, and functional assays showed Tom7 acts inhibitorily at two distinct steps: early Tom40 assembly at SAM (opposing Tom5/Tom6) and late Tom22 integration (via Mdm10 sequestration).","evidence":"Site-specific photocross-linking in yeast, genetic deletion, in vitro assembly kinetics","pmids":["21036907","21059357"],"confidence":"High","gaps":["Structural basis for Tom7's opposing effects at each step unresolved","Mammalian equivalents of the two-step inhibition not demonstrated"]},{"year":2018,"claim":"Tom7 was shown to regulate selective mitochondrial import of Rac1 in endothelial cells, linking TOM complex modulation to redox signaling and cerebrovascular angiogenesis — the first demonstration of a tissue-specific physiological role for Tom7.","evidence":"Zebrafish genetic screen, Tomm7 knockout mice, endothelial-specific rescue, mitochondrial import assays","pmids":["30354240"],"confidence":"Medium","gaps":["Whether Rac1 import regulation is direct or indirect through altered TOM complex composition unclear","Mechanism connecting Rac1 mitochondrial import to redox signaling incompletely defined"]},{"year":2019,"claim":"Tom7 was identified as specifically required for PINK1 import arrest on depolarized mitochondria, with OMA1 acting as the opposing force; this 'tug of war' model explained how the TOM complex acts as a decision point for PINK1 stabilization and mitophagy initiation.","evidence":"Tom7 deletion and OMA1 suppression in mammalian cells, PINK1 transmembrane-domain mutagenesis, cleavage and localization assays","pmids":["30733118"],"confidence":"High","gaps":["Structural basis for how Tom7 retains PINK1 at the outer membrane unknown","Whether Tom7 directly contacts PINK1 or acts indirectly through Tom40 conformation not resolved"]},{"year":2022,"claim":"Identification of biallelic TOMM7 variants (p.Pro29Leu and p.Trp25Arg) as causes of progeroid/syndromic short stature in humans demonstrated that Tom7 is essential for normal development and that its loss causes mitochondrial uncoupling with altered import of oxidative phosphorylation components.","evidence":"Exome sequencing in affected families, quantitative mitochondrial proteomics, respiration assays in patient fibroblasts and Tomm7 mutant mice","pmids":["36282599","36299998"],"confidence":"Medium","gaps":["Only two families reported; genotype-phenotype spectrum remains narrow","Whether mitochondrial uncoupling is a direct consequence of altered import or secondary unclear","Structural impact of missense variants on Tom7–Tom40 interaction not determined"]},{"year":2025,"claim":"TOMM7 was shown to regulate PINK1/Parkin-mediated mitophagy in kidney tubular cells by controlling PLA2G6 redistribution between nucleus and mitochondria, with ZBTB12 identified as a transcriptional repressor of TOMM7, extending Tom7's role to organ-specific damage responses.","evidence":"Tomm7 overexpression in db/db mice, PLA2G6 localization assays, ZBTB12 transcription factor identification","pmids":["41276015"],"confidence":"Medium","gaps":["Whether PLA2G6 is a direct import substrate of the Tom7-modified TOM complex not established","ZBTB12 regulation of TOMM7 confirmed in single system only","Relevance of this pathway to non-renal tissues unknown"]},{"year":null,"claim":"Key unresolved questions include the structural basis for how Tom7 retains PINK1 at the TOM channel, whether Tom7 directly modulates the Tom40 pore conformation versus acting as a steric block, and how tissue-specific import selectivity (Rac1, PLA2G6) is determined by a ubiquitously expressed small subunit.","evidence":"","pmids":[],"confidence":"High","gaps":["No high-resolution structure of Tom7 within the mammalian TOM complex","No reconstituted system demonstrating substrate-selective gating by Tom7","Transcriptional regulation of TOMM7 across tissues poorly characterized"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[0,1,2,6]},{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[0,4,5,6,7]}],"localization":[{"term_id":"GO:0005739","term_label":"mitochondrion","supporting_discovery_ids":[0,1,2,3,5,7]}],"pathway":[{"term_id":"R-HSA-9612973","term_label":"Autophagy","supporting_discovery_ids":[7,11]},{"term_id":"R-HSA-9609507","term_label":"Protein localization","supporting_discovery_ids":[0,1,2,5,6,7]},{"term_id":"R-HSA-1852241","term_label":"Organelle biogenesis and maintenance","supporting_discovery_ids":[4,5,6]}],"complexes":["TOM complex"],"partners":["TOMM40","TOMM22","TOMM5","TOMM6","MDM10","PINK1","OMA1"],"other_free_text":[]},"mechanistic_narrative":"TOMM7 encodes a small tail-anchored subunit of the mitochondrial outer membrane TOM translocase complex that functions as a modulator of complex assembly and a gatekeeper for selective protein import. Its transmembrane segment directly contacts the central pore component Tom40, and Tom7 destabilizes TOM complex assembly at two stages: by antagonizing Tom5/Tom6 during early Tom40 integration at the SAM complex, and by sequestering Mdm10 away from the SAM-Mdm10 complex to delay late Tom22–Tom40 association [PMID:8641278, PMID:21059357, PMID:21036907]. Tom7 is specifically required for PINK1 import arrest on depolarized mitochondria, opposing OMA1-mediated PINK1 cleavage in a regulated tug of war that determines whether PINK1/Parkin-dependent mitophagy is activated [PMID:30733118, PMID:41276015]. Biallelic loss-of-function variants in human TOMM7 cause a progeroid/syndromic short stature disorder characterized by altered mitochondrial protein import, mitochondrial uncoupling, and developmental delay [PMID:36282599, PMID:36299998]."},"prefetch_data":{"uniprot":{"accession":"Q9P0U1","full_name":"Mitochondrial import receptor subunit TOM7 homolog","aliases":["Translocase of outer membrane 7 kDa subunit homolog"],"length_aa":55,"mass_kda":6.2,"function":"Component of the translocase of the outer membrane of mitochondria (TOM) complex essential for the recognition and translocation of cytosolically synthesized mitochondrial preproteins (PubMed:40080546). The TOM complex associates with the ion channel VDAC2 and PINK1 kinase at depolarized mitochondria, this interaction stabilizes PINK1 at the outer mitochondrial membrane and triggers downstream mitophagy by the recruitment of the E3 ubiquitin ligase PRKN (PubMed:40080546)","subcellular_location":"Mitochondrion outer membrane","url":"https://www.uniprot.org/uniprotkb/Q9P0U1/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/TOMM7","classification":"Not Classified","n_dependent_lines":26,"n_total_lines":1208,"dependency_fraction":0.02152317880794702},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"TOMM20A","stoichiometry":10.0}],"url":"https://opencell.sf.czbiohub.org/search/TOMM7","total_profiled":1310},"omim":[{"mim_id":"620601","title":"GARG-MISHRA PROGEROID SYNDROME; GMPGS","url":"https://www.omim.org/entry/620601"},{"mim_id":"616169","title":"TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 5; TOMM5","url":"https://www.omim.org/entry/616169"},{"mim_id":"616168","title":"TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 6; TOMM6","url":"https://www.omim.org/entry/616168"},{"mim_id":"608309","title":"PTEN-INDUCED KINASE 1; PINK1","url":"https://www.omim.org/entry/608309"},{"mim_id":"607980","title":"TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 7; TOMM7","url":"https://www.omim.org/entry/607980"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"","locations":[],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/TOMM7"},"hgnc":{"alias_symbol":["Tom7"],"prev_symbol":[]},"alphafold":{"accession":"Q9P0U1","domains":[{"cath_id":"-","chopping":"9-53","consensus_level":"high","plddt":94.5618,"start":9,"end":53}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9P0U1","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9P0U1-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9P0U1-F1-predicted_aligned_error_v6.png","plddt_mean":92.81},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=TOMM7","jax_strain_url":"https://www.jax.org/strain/search?query=TOMM7"},"sequence":{"accession":"Q9P0U1","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9P0U1.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9P0U1/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9P0U1"}},"corpus_meta":[{"pmid":"30733118","id":"PMC_30733118","title":"Reciprocal Roles of Tom7 and OMA1 during Mitochondrial Import and Activation of PINK1.","date":"2019","source":"Molecular cell","url":"https://pubmed.ncbi.nlm.nih.gov/30733118","citation_count":138,"is_preprint":false},{"pmid":"8641278","id":"PMC_8641278","title":"Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import.","date":"1996","source":"The EMBO journal","url":"https://pubmed.ncbi.nlm.nih.gov/8641278","citation_count":137,"is_preprint":false},{"pmid":"12198123","id":"PMC_12198123","title":"Insertion and assembly of human tom7 into the preprotein translocase complex of the outer mitochondrial membrane.","date":"2002","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/12198123","citation_count":114,"is_preprint":false},{"pmid":"21036907","id":"PMC_21036907","title":"Tom7 regulates Mdm10-mediated assembly of the mitochondrial import channel protein Tom40.","date":"2010","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/21036907","citation_count":87,"is_preprint":false},{"pmid":"16760475","id":"PMC_16760475","title":"Mitochondrial protein sorting: differentiation of beta-barrel assembly by Tom7-mediated segregation of Mdm10.","date":"2006","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/16760475","citation_count":86,"is_preprint":false},{"pmid":"21059357","id":"PMC_21059357","title":"Biogenesis of mitochondria: dual role of Tom7 in modulating assembly of the preprotein translocase of the outer membrane.","date":"2010","source":"Journal of molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/21059357","citation_count":74,"is_preprint":false},{"pmid":"11278536","id":"PMC_11278536","title":"Assembly of Tom6 and Tom7 into the TOM core complex of Neurospora crassa.","date":"2001","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/11278536","citation_count":55,"is_preprint":false},{"pmid":"11943179","id":"PMC_11943179","title":"A conserved proline residue is present in the transmembrane-spanning domain of Tom7 and other tail-anchored protein subunits of the TOM translocase.","date":"2002","source":"FEBS letters","url":"https://pubmed.ncbi.nlm.nih.gov/11943179","citation_count":42,"is_preprint":false},{"pmid":"36282599","id":"PMC_36282599","title":"Autosomal recessive progeroid syndrome due to homozygosity for a TOMM7 variant.","date":"2022","source":"The Journal of clinical investigation","url":"https://pubmed.ncbi.nlm.nih.gov/36282599","citation_count":23,"is_preprint":false},{"pmid":"30354240","id":"PMC_30354240","title":"Endothelial Mitochondrial Preprotein Translocase Tomm7-Rac1 Signaling Axis Dominates Cerebrovascular Network Homeostasis.","date":"2018","source":"Arteriosclerosis, thrombosis, and vascular biology","url":"https://pubmed.ncbi.nlm.nih.gov/30354240","citation_count":18,"is_preprint":false},{"pmid":"36299998","id":"PMC_36299998","title":"A hypomorphic variant in the translocase of the outer mitochondrial membrane complex subunit TOMM7 causes short stature and developmental delay.","date":"2022","source":"HGG advances","url":"https://pubmed.ncbi.nlm.nih.gov/36299998","citation_count":13,"is_preprint":false},{"pmid":"30468788","id":"PMC_30468788","title":"TOM7 silencing exacerbates focal cerebral ischemia injury in rat by targeting PINK1/Beclin1-mediated autophagy.","date":"2018","source":"Behavioural brain research","url":"https://pubmed.ncbi.nlm.nih.gov/30468788","citation_count":12,"is_preprint":false},{"pmid":"25652373","id":"PMC_25652373","title":"[Association of genetic variants in TOMM7 gene and gene environment interaction with type 2 diabetes in Chinese Dong population].","date":"2015","source":"Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences","url":"https://pubmed.ncbi.nlm.nih.gov/25652373","citation_count":3,"is_preprint":false},{"pmid":"41276015","id":"PMC_41276015","title":"Mitochondrial protein TOMM7 alleviates diabetic kidney disease by regulating mitophagy via intracellular redistribution of phospholipase PLA2G6.","date":"2025","source":"Kidney international","url":"https://pubmed.ncbi.nlm.nih.gov/41276015","citation_count":1,"is_preprint":false},{"pmid":"15759864","id":"PMC_15759864","title":"Cloning and characterization of TOM7-like gene in wheat.","date":"2005","source":"Yi chuan xue bao = Acta genetica Sinica","url":"https://pubmed.ncbi.nlm.nih.gov/15759864","citation_count":0,"is_preprint":false},{"pmid":"41460760","id":"PMC_41460760","title":"Growth Hormone Response in a Child With a Homozygous TOMM7 Mutation: Novel Therapeutic Insights.","date":"2025","source":"The American journal of case reports","url":"https://pubmed.ncbi.nlm.nih.gov/41460760","citation_count":0,"is_preprint":false},{"pmid":"41540546","id":"PMC_41540546","title":"Single-cell and Bulk RNA-Seq Analyses Reveal TOMM7-mediated Multi-cell Death Mechanisms Driving Muscle-invasive Bladder Cancer Progression.","date":"2026","source":"Recent patents on anti-cancer drug discovery","url":"https://pubmed.ncbi.nlm.nih.gov/41540546","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.06.10.658840","title":"A CRISPR-CAS9 high throughput machine-learning platform for modulation of genes involved in Parkinson’s disease-associated PINK1-mitophagy in iPSC-derived dopaminergic neurons","date":"2025-06-15","source":"bioRxiv","url":"https://doi.org/10.1101/2025.06.10.658840","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2024.06.27.600933","title":"A genome-wide association study of high-sensitivity C-reactive protein in a large Korean population highlights its role in cholesterol metabolism","date":"2024-06-28","source":"bioRxiv","url":"https://doi.org/10.1101/2024.06.27.600933","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":10576,"output_tokens":3130,"usd":0.039339},"stage2":{"model":"claude-opus-4-6","input_tokens":6503,"output_tokens":2679,"usd":0.149235},"total_usd":0.188574,"stage1_batch_id":"msgbatch_01RPbVc9PDH9zQmYK5Hs6srm","stage2_batch_id":"msgbatch_01JVbVLzeKN2yVrsGp3zC8aM","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1996,\n      \"finding\": \"Tom7 is a small integral membrane subunit of the mitochondrial outer membrane translocase (TOM complex) that destabilizes the interaction between receptors Tom20 and Tom22 and the import pore component Tom40, while Tom6 stabilizes this interaction; deletion of Tom7 inhibits import of outer membrane protein porin and delays two-step import of matrix-destined preproteins, and genetic synthetic lethality of tom7Δ tom20Δ and tom7Δ tom6Δ double mutants confirms functional relationships.\",\n      \"method\": \"Genetic deletion, in vitro import assays, native protein complex analysis, double-mutant synthetic growth defect analysis\",\n      \"journal\": \"The EMBO journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal methods (genetic, biochemical import assays, complex assembly), foundational study replicated by subsequent work\",\n      \"pmids\": [\"8641278\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2001,\n      \"finding\": \"Tom7 in Neurospora crassa is in direct physical contact with the major pore component Tom40, as shown by cross-linking, and its precursor can insert into the outer membrane in vitro and assemble into authentic TOM complexes via a pathway that shares a binding site with the general import pathway and depends on receptor components.\",\n      \"method\": \"Cross-linking, in vitro import and assembly assays, competition assays\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 — in vitro reconstitution of assembly with cross-linking confirming direct Tom40 contact\",\n      \"pmids\": [\"11278536\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2002,\n      \"finding\": \"Human Tom7 is a tail-anchored protein imported into mitochondria in a nucleotide-independent manner, anchored to the outer membrane with its C terminus facing the intermembrane space; it assembles first into an ~120 kDa intermediate containing Tom40 but lacking receptors, then into the ~380 kDa TOM complex additionally containing Tom22; Tom22 is rate-limiting for this final assembly step.\",\n      \"method\": \"In vitro import into HeLa mitochondria, blue native electrophoresis, supershift antibody analysis, Tom22 overexpression\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal biochemical methods in human cells with functional overexpression validation\",\n      \"pmids\": [\"12198123\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2002,\n      \"finding\": \"Tom7 is a tail-anchored protein whose carboxy-terminal 33 amino acids contain mitochondrial outer membrane targeting information, and a conserved proline residue within the transmembrane segment is required for efficient targeting to the outer membrane.\",\n      \"method\": \"Deletion/truncation mutagenesis, proline point mutation, subcellular targeting assays\",\n      \"journal\": \"FEBS letters\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — mutagenesis with targeting readout, single lab\",\n      \"pmids\": [\"11943179\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2006,\n      \"finding\": \"Tom7 promotes segregation of the SAM complex subunit Mdm10 into a low-molecular-mass form away from the SAM(holo) complex; deletion of Tom7 increases the fraction of Mdm10 in the SAM(holo) complex, explaining the opposing roles of Tom7 (promotes porin assembly, antagonizes Tom40 assembly) versus Mdm10 (promotes Tom40 assembly).\",\n      \"method\": \"Genetic deletion, co-immunoprecipitation, native gel electrophoresis, in vitro import/assembly assays\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — genetic and biochemical orthogonal methods with clear epistatic placement of Tom7 relative to Mdm10 and SAM complex\",\n      \"pmids\": [\"16760475\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"Tom7 directly interacts with Tom40 through its transmembrane segment and with Mdm10, as shown by site-specific photocross-linking in vivo; Tom7 recruits Mdm10 to enhance its association with the MMM1 complex and regulates the timing of Tom40 release from the TOB/SAM complex for subsequent assembly into the TOM40 complex.\",\n      \"method\": \"Site-specific photocross-linking in vivo, in vitro import assays, Tom7 overexpression/depletion\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 — in vivo site-specific cross-linking directly demonstrating protein contacts, complemented by functional import assays\",\n      \"pmids\": [\"21036907\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"Tom7 plays inhibitory roles at two distinct steps in TOM complex biogenesis: (1) antagonizing Tom5 and Tom6 at an early stage of Tom40 assembly at the SAM complex, and (2) interacting with Mdm10 not bound to the SAM complex to promote dissociation of the SAM-Mdm10 complex, thereby delaying assembly of Tom22 with Tom40 at a late stage.\",\n      \"method\": \"Genetic deletion, native gel electrophoresis, in vitro import assays, complex assembly tracking\",\n      \"journal\": \"Journal of molecular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal biochemical steps dissected, consistent with and extending prior studies\",\n      \"pmids\": [\"21059357\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Tom7 is required for PINK1 import arrest at the outer mitochondrial membrane upon mitochondrial depolarization; deletion of Tom7 causes PINK1 to be imported into depolarized mitochondria and cleaved by the OMA1 protease rather than accumulating at the outer membrane. A negatively charged amino acid cluster motif just C-terminal to the PINK1 transmembrane domain mediates this retention, and Tom7 and OMA1 act in a 'tug of war' to determine PINK1 fate.\",\n      \"method\": \"Tom7 deletion, OMA1 suppression, mutagenesis of PINK1 motif, PINK1 localization and cleavage assays\",\n      \"journal\": \"Molecular cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — genetic and biochemical epistasis with mutagenesis, highly cited foundational study replicated across multiple conditions\",\n      \"pmids\": [\"30733118\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Tomm7 in endothelial cells controls cerebrovascular network formation by regulating the mitochondrial import of Rac1; Tomm7 deficiency causes increased import of Rac1 into mitochondria, activating mitochondrial Rac1-coupled redox signaling that impairs angiogenesis and underlies cerebrovascular malformation.\",\n      \"method\": \"Zebrafish loss-of-function genetic screen, Tomm7 knockout mice, endothelial-specific transgenic rescue, mitochondrial import assays, vascular imaging\",\n      \"journal\": \"Arteriosclerosis, thrombosis, and vascular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — multiple model organisms and genetic rescue, but mechanistic link to Rac1 import based on single lab\",\n      \"pmids\": [\"30354240\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"A homozygous missense variant (p.Pro29Leu) in human TOMM7 causes a progeroid syndrome with severe growth retardation; proband-derived fibroblasts show altered mitochondrial protein import with increased abundance of oxidative phosphorylation proteins and reduced phospholipid metabolism proteins, and elevated basal and maximal oxygen consumption rates.\",\n      \"method\": \"Exome sequencing, quantitative mitochondrial proteomics, oxygen consumption rate measurement in patient fibroblasts\",\n      \"journal\": \"The Journal of clinical investigation\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — patient variant with proteomics and functional metabolic readout, single family report\",\n      \"pmids\": [\"36282599\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"A homozygous hypomorphic variant in TOMM7 (p.Trp25Arg) causes syndromic short stature and developmental delay; Tomm7 mutant mice show mitochondrial uncoupling with increased oxygen consumption but normal ETC function, suggesting Tomm7 deficiency uncouples oxidation from ATP synthesis without impairing TCA cycle or ETC.\",\n      \"method\": \"Mouse knockout and knock-in models, oxygen consumption assays with ETC inhibitors, phenotypic characterization\",\n      \"journal\": \"HGG advances\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — mouse models with functional mitochondrial assays, single lab\",\n      \"pmids\": [\"36299998\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"TOMM7 regulates PINK1/Parkin-mediated mitophagy in kidney tubular cells by modulating the intracellular redistribution of phospholipase PLA2G6 between the nucleus and mitochondria; TOMM7 overexpression in db/db mice restores PINK1/Parkin-mediated mitophagy and alleviates tubular injury. ZBTB12 was identified as a transcriptional repressor of TOMM7.\",\n      \"method\": \"Tomm7 overexpression in db/db mice, PLA2G6 localization assays, ZBTB12 transcription factor identification, tubular cell in vitro models\",\n      \"journal\": \"Kidney international\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — in vivo overexpression with mechanistic follow-up on PLA2G6 redistribution, single lab\",\n      \"pmids\": [\"41276015\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"CRISPR knockout of TOM7 in human iPSC-derived dopaminergic neurons decreases ubiquitin pSer65 upregulation during mitophagy activation, confirming Tom7's role in the PINK1-PARKIN mitophagy pathway in a human neuronal model.\",\n      \"method\": \"High-throughput arrayed CRISPR-Cas9 screen, high-content immunofluorescence imaging, machine learning analysis in iPSC-derived dopaminergic neurons\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — functional genomic screen in disease-relevant human neuronal model, preprint\",\n      \"pmids\": [\"bio_10.1101_2025.06.10.658840\"],\n      \"is_preprint\": true\n    }\n  ],\n  \"current_model\": \"TOMM7 encodes a small tail-anchored integral membrane subunit of the mitochondrial outer membrane TOM translocase complex that directly contacts Tom40 via its transmembrane segment, destabilizes TOM complex assembly by antagonizing Tom5/Tom6 and by segregating Mdm10 from the SAM-Mdm10 complex, is specifically required for PINK1 import arrest on depolarized mitochondria (opposing OMA1-mediated PINK1 cleavage in a regulated 'tug of war'), and regulates PINK1/Parkin-dependent mitophagy as well as selective import of substrates such as Rac1 and PLA2G6, thereby controlling mitochondrial homeostasis, angiogenesis, and cellular responses to damage.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"TOMM7 encodes a small tail-anchored subunit of the mitochondrial outer membrane TOM translocase complex that functions as a modulator of complex assembly and a gatekeeper for selective protein import. Its transmembrane segment directly contacts the central pore component Tom40, and Tom7 destabilizes TOM complex assembly at two stages: by antagonizing Tom5/Tom6 during early Tom40 integration at the SAM complex, and by sequestering Mdm10 away from the SAM-Mdm10 complex to delay late Tom22–Tom40 association [PMID:8641278, PMID:21059357, PMID:21036907]. Tom7 is specifically required for PINK1 import arrest on depolarized mitochondria, opposing OMA1-mediated PINK1 cleavage in a regulated tug of war that determines whether PINK1/Parkin-dependent mitophagy is activated [PMID:30733118, PMID:41276015]. Biallelic loss-of-function variants in human TOMM7 cause a progeroid/syndromic short stature disorder characterized by altered mitochondrial protein import, mitochondrial uncoupling, and developmental delay [PMID:36282599, PMID:36299998].\",\n  \"teleology\": [\n    {\n      \"year\": 1996,\n      \"claim\": \"Identification of Tom7 as a small TOM complex subunit with a destabilizing role in receptor–pore interactions established that TOM assembly is actively modulated rather than merely driven by affinity, and that Tom7 opposes Tom6 function.\",\n      \"evidence\": \"Yeast gene deletion with in vitro import assays, native complex analysis, and synthetic lethality (tom7Δ tom20Δ, tom7Δ tom6Δ)\",\n      \"pmids\": [\"8641278\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Direct physical contacts between Tom7 and other TOM subunits not yet mapped\",\n        \"Mechanism of how Tom7 destabilizes receptor–pore interaction unknown\"\n      ]\n    },\n    {\n      \"year\": 2001,\n      \"claim\": \"Cross-linking experiments resolved that Tom7 makes direct physical contact with Tom40 through its transmembrane domain, establishing that Tom7 acts on the pore itself rather than indirectly through receptors.\",\n      \"evidence\": \"Chemical cross-linking and in vitro assembly/competition assays in Neurospora crassa mitochondria\",\n      \"pmids\": [\"11278536\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Residue-level contacts not defined\",\n        \"Whether human Tom7 contacts Tom40 identically was unconfirmed\"\n      ]\n    },\n    {\n      \"year\": 2002,\n      \"claim\": \"Characterization of human Tom7 as a tail-anchored protein that assembles stepwise into TOM complexes via a ~120 kDa Tom40-containing intermediate before joining the ~380 kDa holo-complex established the assembly pathway in mammalian cells and identified Tom22 as rate-limiting for the final step.\",\n      \"evidence\": \"In vitro import into HeLa mitochondria, blue native PAGE, antibody supershift, Tom22 overexpression\",\n      \"pmids\": [\"12198123\", \"11943179\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Functional consequences of Tom7 loss in human cells not yet tested\",\n        \"Role of the conserved transmembrane proline in assembly kinetics not fully resolved\"\n      ]\n    },\n    {\n      \"year\": 2006,\n      \"claim\": \"Discovery that Tom7 promotes segregation of Mdm10 away from the SAM(holo) complex explained its paradoxical dual role — promoting porin assembly while antagonizing Tom40 assembly — by placing Tom7 as a regulator of SAM complex composition.\",\n      \"evidence\": \"Yeast genetic deletion, co-immunoprecipitation, native gel electrophoresis, in vitro import/assembly\",\n      \"pmids\": [\"16760475\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Direct Tom7–Mdm10 interaction not yet proven by cross-linking\",\n        \"Whether Mdm10 regulation is conserved in mammals unknown\"\n      ]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"In vivo site-specific photocross-linking confirmed that Tom7 contacts both Tom40 (via its transmembrane segment) and Mdm10, and functional assays showed Tom7 acts inhibitorily at two distinct steps: early Tom40 assembly at SAM (opposing Tom5/Tom6) and late Tom22 integration (via Mdm10 sequestration).\",\n      \"evidence\": \"Site-specific photocross-linking in yeast, genetic deletion, in vitro assembly kinetics\",\n      \"pmids\": [\"21036907\", \"21059357\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural basis for Tom7's opposing effects at each step unresolved\",\n        \"Mammalian equivalents of the two-step inhibition not demonstrated\"\n      ]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Tom7 was shown to regulate selective mitochondrial import of Rac1 in endothelial cells, linking TOM complex modulation to redox signaling and cerebrovascular angiogenesis — the first demonstration of a tissue-specific physiological role for Tom7.\",\n      \"evidence\": \"Zebrafish genetic screen, Tomm7 knockout mice, endothelial-specific rescue, mitochondrial import assays\",\n      \"pmids\": [\"30354240\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Whether Rac1 import regulation is direct or indirect through altered TOM complex composition unclear\",\n        \"Mechanism connecting Rac1 mitochondrial import to redox signaling incompletely defined\"\n      ]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Tom7 was identified as specifically required for PINK1 import arrest on depolarized mitochondria, with OMA1 acting as the opposing force; this 'tug of war' model explained how the TOM complex acts as a decision point for PINK1 stabilization and mitophagy initiation.\",\n      \"evidence\": \"Tom7 deletion and OMA1 suppression in mammalian cells, PINK1 transmembrane-domain mutagenesis, cleavage and localization assays\",\n      \"pmids\": [\"30733118\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural basis for how Tom7 retains PINK1 at the outer membrane unknown\",\n        \"Whether Tom7 directly contacts PINK1 or acts indirectly through Tom40 conformation not resolved\"\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Identification of biallelic TOMM7 variants (p.Pro29Leu and p.Trp25Arg) as causes of progeroid/syndromic short stature in humans demonstrated that Tom7 is essential for normal development and that its loss causes mitochondrial uncoupling with altered import of oxidative phosphorylation components.\",\n      \"evidence\": \"Exome sequencing in affected families, quantitative mitochondrial proteomics, respiration assays in patient fibroblasts and Tomm7 mutant mice\",\n      \"pmids\": [\"36282599\", \"36299998\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Only two families reported; genotype-phenotype spectrum remains narrow\",\n        \"Whether mitochondrial uncoupling is a direct consequence of altered import or secondary unclear\",\n        \"Structural impact of missense variants on Tom7–Tom40 interaction not determined\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"TOMM7 was shown to regulate PINK1/Parkin-mediated mitophagy in kidney tubular cells by controlling PLA2G6 redistribution between nucleus and mitochondria, with ZBTB12 identified as a transcriptional repressor of TOMM7, extending Tom7's role to organ-specific damage responses.\",\n      \"evidence\": \"Tomm7 overexpression in db/db mice, PLA2G6 localization assays, ZBTB12 transcription factor identification\",\n      \"pmids\": [\"41276015\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Whether PLA2G6 is a direct import substrate of the Tom7-modified TOM complex not established\",\n        \"ZBTB12 regulation of TOMM7 confirmed in single system only\",\n        \"Relevance of this pathway to non-renal tissues unknown\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Key unresolved questions include the structural basis for how Tom7 retains PINK1 at the TOM channel, whether Tom7 directly modulates the Tom40 pore conformation versus acting as a steric block, and how tissue-specific import selectivity (Rac1, PLA2G6) is determined by a ubiquitously expressed small subunit.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"No high-resolution structure of Tom7 within the mammalian TOM complex\",\n        \"No reconstituted system demonstrating substrate-selective gating by Tom7\",\n        \"Transcriptional regulation of TOMM7 across tissues poorly characterized\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [0, 1, 2, 6]},\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [0, 4, 5, 6, 7]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005739\", \"supporting_discovery_ids\": [0, 1, 2, 3, 5, 7]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-9612973\", \"supporting_discovery_ids\": [7, 11]},\n      {\"term_id\": \"R-HSA-9609507\", \"supporting_discovery_ids\": [0, 1, 2, 5, 6, 7]},\n      {\"term_id\": \"R-HSA-1852241\", \"supporting_discovery_ids\": [4, 5, 6]}\n    ],\n    \"complexes\": [\n      \"TOM complex\"\n    ],\n    \"partners\": [\n      \"TOMM40\",\n      \"TOMM22\",\n      \"TOMM5\",\n      \"TOMM6\",\n      \"MDM10\",\n      \"PINK1\",\n      \"OMA1\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```"}