{"gene":"TMSB10","run_date":"2026-06-10T10:51:55","timeline":{"discoveries":[{"year":2022,"finding":"Tmsb10 promotes fetal Leydig cell (FLC) differentiation from progenitor cells by suppressing the RAS/ERK signaling pathway. PDGF regulates ciliogenesis through RAS/ERK and PI3K/AKT pathways to promote DHH-dependent FLC differentiation, and transiently expressed Tmsb10 in FLC progenitors induces their differentiation into FLCs by suppressing RAS/ERK.","method":"Single-cell RNA sequencing to identify Tmsb10 expression in progenitors; functional studies in mouse fetal testis model with pathway analysis (RAS/ERK, PI3K/AKT); gene knockout/manipulation with defined cellular phenotype readout (FLC differentiation)","journal":"Communications biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — scRNA-seq for identification plus functional knockout with defined cellular phenotype and pathway placement in single lab study","pmids":["36109592"],"is_preprint":false},{"year":2024,"finding":"Urolithin A (UA) promotes degradation of TMSB10 protein via the autophagy-lysosome pathway. Reduction of TMSB10 inhibits F-actin formation for cell migration by disrupting the equilibrium between G-actin-TMSB10 and G-actin-ATP interactions, thereby suppressing NSCLC cell proliferation, migration, and invasion.","method":"Proteomics to identify downstream factors; TMSB10 knockdown/overexpression with proliferation/transwell assays; confocal imaging, GST pull-down, and western blotting to investigate mechanism of UA-induced TMSB10 degradation","journal":"Phytomedicine : international journal of phytotherapy and phytopharmacology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (GST pull-down, confocal, western blot, KD/OE phenotype) in single lab study establishing G-actin binding and autophagy-lysosome degradation","pmids":["39368341"],"is_preprint":false},{"year":2020,"finding":"DNMT1 maintains methylation of the miR-152-3p promoter, preventing miR-152-3p from targeting and suppressing TMSB10 expression. Silencing DNMT1 leads to demethylation of miR-152-3p, upregulation of miR-152-3p, and consequent reduction of TMSB10 expression, suppressing colorectal cancer cell progression and tumor growth.","method":"Methylation detection of miR-152-3p in CRC tissues/cells; transfection experiments with DNMT1 or miR-152-3p constructs in SW-480 and HCT-116 cells; binding/targeting relationship analysis; in vivo tumor growth assays","journal":"IUBMB life","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct targeting relationship established with functional rescue experiments and in vivo validation, single lab with two orthogonal approaches (methylation analysis + functional assays)","pmids":["32918845"],"is_preprint":false},{"year":2020,"finding":"TMSB10 knockdown in ccRCC cells impairs proliferation, migration, and invasion, and reduces phosphorylation of PI3K and expression of VEGF, placing TMSB10 upstream of the PI3K/VEGF signaling axis in clear cell renal cell carcinoma.","method":"TMSB10 knockdown in ccRCC cell lines with proliferation, migration, and invasion assays; western blotting for PI3K phosphorylation and VEGF expression","journal":"International journal of oncology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single knockdown approach with pathway readout but no reconstitution or epistasis confirmation","pmids":["32319572"],"is_preprint":false},{"year":2022,"finding":"JUN transcription factor binds to the promoter region of TMSB10 and regulates its expression; JUN-driven high expression of TMSB10 promotes ccRCC cell proliferation and inhibits apoptosis.","method":"JASPAR database prediction of JUN binding sites in TMSB10 promoter; ChIP experiment to confirm JUN binding; qRT-PCR for mRNA levels; proliferation and apoptosis functional assays in ccRCC cell lines","journal":"Annals of clinical and laboratory science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — ChIP experiment directly confirms JUN binding to TMSB10 promoter, combined with functional assays, single lab","pmids":["35414502"],"is_preprint":false},{"year":2025,"finding":"TMSB10 knockdown in fibroblasts and in a diabetic mouse model reduces expression of fibrosis markers (Fn1, Col1a1, α-Sma by ~50-70%) and attenuates ECM accumulation; mechanistically, TMSB10 deficiency suppresses phosphorylation of SMAD2/3, identifying TMSB10 as a positive regulator of TGF-β/SMAD signaling in renal fibroblasts.","method":"Tmsb10 knockdown in NIH-3T3 fibroblasts and in a diabetic mouse model; assessment of fibrosis markers by western blot/qPCR; ECM deposition analysis; SMAD2/3 phosphorylation measured; single-cell RNA sequencing for initial identification","journal":"Diabetes, metabolic syndrome and obesity : targets and therapy","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — in vivo and in vitro KD with defined molecular readout (SMAD2/3 phosphorylation) and pathway placement; single lab","pmids":["41497884"],"is_preprint":false},{"year":2025,"finding":"TMSB10 silencing in prostate cancer cell lines (LNCaP and DU145) suppresses cell proliferation, migration, and invasion, while overexpression enhances these processes. In co-culture experiments, TMSB10 overexpression skews macrophage polarization toward M2-type (decreasing M1, increasing M2), reducing immune cell cytotoxicity and altering cytokine secretion.","method":"TMSB10 siRNA knockdown and overexpression in prostate cancer cell lines; proliferation, migration, invasion assays; co-culture experiments with macrophages measuring M1/M2 polarization and cytokine secretion","journal":"Molecular medicine (Cambridge, Mass.)","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, functional KD/OE with co-culture readout but no molecular mechanism for macrophage polarization identified","pmids":["40307738"],"is_preprint":false},{"year":2024,"finding":"The UTR of TMSB10 significantly enhances mRNA expression of reporter genes in antigen-presenting cells (dendritic cell subtypes) and in vivo, identified through high TMSB10 mRNA abundance in dendritic cells from GEO database analysis. This UTR-driven enhanced expression leads to improved humoral and cellular immune responses when used in mRNA vaccine constructs.","method":"GEO database mining to identify TMSB10 high expression in dendritic cells; reporter gene assays in vitro in APC and 293T cells; in vivo mRNA vaccine experiments measuring IgG titers, IFN-γ, IL-4, CD4+/CD8+ T cell proliferation","journal":"Vaccines","confidence":"Low","confidence_rationale":"Tier 3 / Weak — functional UTR activity confirmed in reporter assays but mechanism of high mRNA abundance in dendritic cells not mechanistically dissected; single lab","pmids":["38675814"],"is_preprint":false}],"current_model":"TMSB10 (thymosin β10) is a G-actin sequestering protein that suppresses F-actin polymerization; it promotes cancer cell proliferation, migration, and invasion across multiple tumor types by modulating actin dynamics (disrupting G-actin-ATP interactions), activating PI3K/VEGF signaling, and driving TGF-β/SMAD2/3-dependent fibroblast activation; its expression is transcriptionally regulated by JUN and epigenetically controlled via DNMT1-mediated methylation of miR-152-3p; in fetal testis, Tmsb10 transiently expressed in Leydig cell progenitors suppresses RAS/ERK signaling to drive fetal Leydig cell differentiation cooperatively with DHH and PDGF signaling."},"narrative":{"mechanistic_narrative":"TMSB10 (thymosin β10) is a G-actin-binding protein that governs actin dynamics to drive cell proliferation, migration, and invasion across multiple cancers [PMID:39368341, PMID:32319572]. Mechanistically, TMSB10 binds G-actin and disrupts the equilibrium between G-actin-TMSB10 and G-actin-ATP interactions, controlling F-actin formation required for cell migration; its degradation via the autophagy-lysosome pathway suppresses NSCLC proliferation, migration, and invasion [PMID:39368341]. In clear cell renal cell carcinoma, TMSB10 acts upstream of a PI3K/VEGF signaling axis, with knockdown reducing PI3K phosphorylation and VEGF expression [PMID:32319572]. TMSB10 expression is controlled both transcriptionally, through JUN binding to its promoter [PMID:35414502], and epigenetically, through DNMT1-maintained methylation of the miR-152-3p promoter that otherwise targets and suppresses TMSB10 [PMID:32918845]. Beyond cancer, TMSB10 is a positive regulator of TGF-β/SMAD signaling, promoting SMAD2/3 phosphorylation and ECM accumulation in renal fibroblasts [PMID:41497884], and in fetal testis it transiently marks Leydig cell progenitors where it suppresses RAS/ERK signaling to drive fetal Leydig cell differentiation [PMID:36109592].","teleology":[{"year":2020,"claim":"Established that TMSB10 functions upstream of an oncogenic signaling axis, addressing how its expression translates into tumor cell behavior.","evidence":"TMSB10 knockdown in ccRCC cell lines with proliferation/migration/invasion assays and western blotting for PI3K phosphorylation and VEGF","pmids":["32319572"],"confidence":"Low","gaps":["Single knockdown approach without reconstitution or epistasis confirmation","Does not establish whether PI3K/VEGF effects are direct or downstream of actin changes","No mechanism linking TMSB10 to PI3K activation"]},{"year":2020,"claim":"Identified an epigenetic control circuit explaining how TMSB10 is maintained at high levels in cancer, via DNMT1/miR-152-3p.","evidence":"Methylation detection, DNMT1/miR-152-3p transfection and targeting analysis in CRC cells with in vivo tumor growth assays","pmids":["32918845"],"confidence":"Medium","gaps":["Direct binding of miR-152-3p to the TMSB10 transcript inferred from targeting analysis","Does not address whether this circuit operates outside colorectal cancer"]},{"year":2022,"claim":"Defined a developmental role distinct from cancer, showing TMSB10 drives fetal Leydig cell differentiation by suppressing RAS/ERK.","evidence":"scRNA-seq identification plus functional manipulation in mouse fetal testis with RAS/ERK and PI3K/AKT pathway analysis","pmids":["36109592"],"confidence":"Medium","gaps":["Molecular mechanism by which TMSB10 suppresses RAS/ERK not resolved","Relationship between actin-binding activity and ERK suppression unclear"]},{"year":2022,"claim":"Identified JUN as a direct transcriptional activator of TMSB10, providing an upstream determinant of its oncogenic expression.","evidence":"ChIP confirmation of JUN binding to the TMSB10 promoter with qRT-PCR and proliferation/apoptosis assays in ccRCC cells","pmids":["35414502"],"confidence":"Medium","gaps":["Does not establish whether JUN regulation interacts with the DNMT1/miR-152-3p axis","Single lab, single tumor type"]},{"year":2024,"claim":"Resolved the core actin-related mechanism, showing TMSB10 binds G-actin and that its autophagic degradation disrupts F-actin formation for migration.","evidence":"GST pull-down, confocal imaging, western blotting, and TMSB10 KD/OE with proliferation/transwell assays in NSCLC; Urolithin A as a degradation inducer","pmids":["39368341"],"confidence":"Medium","gaps":["Structural basis of G-actin-TMSB10 binding not determined","Autophagy-lysosome degradation mechanism characterized only via Urolithin A treatment"]},{"year":2024,"claim":"Showed the TMSB10 UTR confers high mRNA expression in antigen-presenting cells, a property exploitable for mRNA vaccine design.","evidence":"GEO mining, reporter assays in APCs/293T, and in vivo mRNA vaccine immune readouts","pmids":["38675814"],"confidence":"Low","gaps":["Mechanism of high TMSB10 mRNA abundance in dendritic cells not dissected","Concerns the UTR element rather than TMSB10 protein function"]},{"year":2025,"claim":"Extended TMSB10 function beyond cancer to fibrosis, positioning it as a positive regulator of TGF-β/SMAD2/3 signaling.","evidence":"Tmsb10 knockdown in NIH-3T3 fibroblasts and a diabetic mouse model with fibrosis marker and SMAD2/3 phosphorylation readouts; scRNA-seq for identification","pmids":["41497884"],"confidence":"Medium","gaps":["Mechanism linking TMSB10 to SMAD2/3 phosphorylation not defined","Single lab; relationship to actin-binding activity unaddressed"]},{"year":2025,"claim":"Linked TMSB10 to immune microenvironment remodeling, showing it skews macrophages toward an M2 phenotype in prostate cancer.","evidence":"siRNA knockdown and overexpression in prostate cancer cell lines with co-culture macrophage polarization and cytokine assays","pmids":["40307738"],"confidence":"Low","gaps":["No molecular mechanism identified for macrophage polarization","Co-culture readout without in vivo immune validation"]},{"year":null,"claim":"How TMSB10's single G-actin-binding activity mechanistically converges on the diverse signaling outputs (PI3K/VEGF, RAS/ERK, TGF-β/SMAD) attributed to it remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No unifying mechanism connecting actin sequestration to specific signaling cascades","No structural model of TMSB10 in complex with partners","Tissue-specific determinants of opposing roles (differentiation vs. proliferation) unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[1]}],"localization":[{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[1]}],"pathway":[{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[0,3,5]}],"complexes":[],"partners":["ACTB"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P63313","full_name":"Thymosin beta-10","aliases":[],"length_aa":44,"mass_kda":5.0,"function":"Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity)","subcellular_location":"Cytoplasm, cytoskeleton","url":"https://www.uniprot.org/uniprotkb/P63313/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/TMSB10","classification":"Common Essential","n_dependent_lines":437,"n_total_lines":1090,"dependency_fraction":0.40091743119266054},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"ACTB","stoichiometry":10.0},{"gene":"GSTP1","stoichiometry":4.0},{"gene":"INPPL1","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/TMSB10","total_profiled":1310},"omim":[{"mim_id":"188399","title":"THYMOSIN, BETA-10; TMSB10","url":"https://www.omim.org/entry/188399"}],"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/TMSB10"},"hgnc":{"alias_symbol":["TB10"],"prev_symbol":[]},"alphafold":{"accession":"P63313","domains":[{"cath_id":"-","chopping":"6-42","consensus_level":"medium","plddt":75.0389,"start":6,"end":42}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P63313","model_url":"https://alphafold.ebi.ac.uk/files/AF-P63313-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P63313-F1-predicted_aligned_error_v6.png","plddt_mean":73.06},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=TMSB10","jax_strain_url":"https://www.jax.org/strain/search?query=TMSB10"},"sequence":{"accession":"P63313","fasta_url":"https://rest.uniprot.org/uniprotkb/P63313.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P63313/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P63313"}},"corpus_meta":[{"pmid":"15879133","id":"PMC_15879133","title":"Exchanging ESAT6 with TB10.4 in an Ag85B 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a TMSB10-driven cell state for non-invasive assessment and precision stratification in breast cancer.","date":"2026","source":"Frontiers in immunology","url":"https://pubmed.ncbi.nlm.nih.gov/42088484","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.03.21.644506","title":"Fibrillarin shapes oncogenic protein pools and ribosomal composition in triple-negative breast cancer","date":"2025-03-23","source":"bioRxiv","url":"https://doi.org/10.1101/2025.03.21.644506","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2024.11.19.624204","title":"Early-Life Systemic Inflammation Modulate Microglia Phenotype to Slow Down Aβ Pathology in the 5xFAD Mouse Model of Alzheimer’s Disease","date":"2024-11-19","source":"bioRxiv","url":"https://doi.org/10.1101/2024.11.19.624204","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":26027,"output_tokens":2378,"usd":0.056876,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":9500,"output_tokens":2784,"usd":0.05855,"stage2_stop_reason":"end_turn"},"total_usd":0.115426,"stage1_batch_id":"msgbatch_017qqVz33Ga63SCDwzb35XPb","stage2_batch_id":"msgbatch_01Scr2Ei9x4HJMiRGxwrmvLK","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2022,\n      \"finding\": \"Tmsb10 promotes fetal Leydig cell (FLC) differentiation from progenitor cells by suppressing the RAS/ERK signaling pathway. PDGF regulates ciliogenesis through RAS/ERK and PI3K/AKT pathways to promote DHH-dependent FLC differentiation, and transiently expressed Tmsb10 in FLC progenitors induces their differentiation into FLCs by suppressing RAS/ERK.\",\n      \"method\": \"Single-cell RNA sequencing to identify Tmsb10 expression in progenitors; functional studies in mouse fetal testis model with pathway analysis (RAS/ERK, PI3K/AKT); gene knockout/manipulation with defined cellular phenotype readout (FLC differentiation)\",\n      \"journal\": \"Communications biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — scRNA-seq for identification plus functional knockout with defined cellular phenotype and pathway placement in single lab study\",\n      \"pmids\": [\"36109592\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"Urolithin A (UA) promotes degradation of TMSB10 protein via the autophagy-lysosome pathway. Reduction of TMSB10 inhibits F-actin formation for cell migration by disrupting the equilibrium between G-actin-TMSB10 and G-actin-ATP interactions, thereby suppressing NSCLC cell proliferation, migration, and invasion.\",\n      \"method\": \"Proteomics to identify downstream factors; TMSB10 knockdown/overexpression with proliferation/transwell assays; confocal imaging, GST pull-down, and western blotting to investigate mechanism of UA-induced TMSB10 degradation\",\n      \"journal\": \"Phytomedicine : international journal of phytotherapy and phytopharmacology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (GST pull-down, confocal, western blot, KD/OE phenotype) in single lab study establishing G-actin binding and autophagy-lysosome degradation\",\n      \"pmids\": [\"39368341\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"DNMT1 maintains methylation of the miR-152-3p promoter, preventing miR-152-3p from targeting and suppressing TMSB10 expression. Silencing DNMT1 leads to demethylation of miR-152-3p, upregulation of miR-152-3p, and consequent reduction of TMSB10 expression, suppressing colorectal cancer cell progression and tumor growth.\",\n      \"method\": \"Methylation detection of miR-152-3p in CRC tissues/cells; transfection experiments with DNMT1 or miR-152-3p constructs in SW-480 and HCT-116 cells; binding/targeting relationship analysis; in vivo tumor growth assays\",\n      \"journal\": \"IUBMB life\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct targeting relationship established with functional rescue experiments and in vivo validation, single lab with two orthogonal approaches (methylation analysis + functional assays)\",\n      \"pmids\": [\"32918845\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"TMSB10 knockdown in ccRCC cells impairs proliferation, migration, and invasion, and reduces phosphorylation of PI3K and expression of VEGF, placing TMSB10 upstream of the PI3K/VEGF signaling axis in clear cell renal cell carcinoma.\",\n      \"method\": \"TMSB10 knockdown in ccRCC cell lines with proliferation, migration, and invasion assays; western blotting for PI3K phosphorylation and VEGF expression\",\n      \"journal\": \"International journal of oncology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single knockdown approach with pathway readout but no reconstitution or epistasis confirmation\",\n      \"pmids\": [\"32319572\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"JUN transcription factor binds to the promoter region of TMSB10 and regulates its expression; JUN-driven high expression of TMSB10 promotes ccRCC cell proliferation and inhibits apoptosis.\",\n      \"method\": \"JASPAR database prediction of JUN binding sites in TMSB10 promoter; ChIP experiment to confirm JUN binding; qRT-PCR for mRNA levels; proliferation and apoptosis functional assays in ccRCC cell lines\",\n      \"journal\": \"Annals of clinical and laboratory science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — ChIP experiment directly confirms JUN binding to TMSB10 promoter, combined with functional assays, single lab\",\n      \"pmids\": [\"35414502\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"TMSB10 knockdown in fibroblasts and in a diabetic mouse model reduces expression of fibrosis markers (Fn1, Col1a1, α-Sma by ~50-70%) and attenuates ECM accumulation; mechanistically, TMSB10 deficiency suppresses phosphorylation of SMAD2/3, identifying TMSB10 as a positive regulator of TGF-β/SMAD signaling in renal fibroblasts.\",\n      \"method\": \"Tmsb10 knockdown in NIH-3T3 fibroblasts and in a diabetic mouse model; assessment of fibrosis markers by western blot/qPCR; ECM deposition analysis; SMAD2/3 phosphorylation measured; single-cell RNA sequencing for initial identification\",\n      \"journal\": \"Diabetes, metabolic syndrome and obesity : targets and therapy\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — in vivo and in vitro KD with defined molecular readout (SMAD2/3 phosphorylation) and pathway placement; single lab\",\n      \"pmids\": [\"41497884\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"TMSB10 silencing in prostate cancer cell lines (LNCaP and DU145) suppresses cell proliferation, migration, and invasion, while overexpression enhances these processes. In co-culture experiments, TMSB10 overexpression skews macrophage polarization toward M2-type (decreasing M1, increasing M2), reducing immune cell cytotoxicity and altering cytokine secretion.\",\n      \"method\": \"TMSB10 siRNA knockdown and overexpression in prostate cancer cell lines; proliferation, migration, invasion assays; co-culture experiments with macrophages measuring M1/M2 polarization and cytokine secretion\",\n      \"journal\": \"Molecular medicine (Cambridge, Mass.)\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, functional KD/OE with co-culture readout but no molecular mechanism for macrophage polarization identified\",\n      \"pmids\": [\"40307738\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"The UTR of TMSB10 significantly enhances mRNA expression of reporter genes in antigen-presenting cells (dendritic cell subtypes) and in vivo, identified through high TMSB10 mRNA abundance in dendritic cells from GEO database analysis. This UTR-driven enhanced expression leads to improved humoral and cellular immune responses when used in mRNA vaccine constructs.\",\n      \"method\": \"GEO database mining to identify TMSB10 high expression in dendritic cells; reporter gene assays in vitro in APC and 293T cells; in vivo mRNA vaccine experiments measuring IgG titers, IFN-γ, IL-4, CD4+/CD8+ T cell proliferation\",\n      \"journal\": \"Vaccines\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — functional UTR activity confirmed in reporter assays but mechanism of high mRNA abundance in dendritic cells not mechanistically dissected; single lab\",\n      \"pmids\": [\"38675814\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"TMSB10 (thymosin β10) is a G-actin sequestering protein that suppresses F-actin polymerization; it promotes cancer cell proliferation, migration, and invasion across multiple tumor types by modulating actin dynamics (disrupting G-actin-ATP interactions), activating PI3K/VEGF signaling, and driving TGF-β/SMAD2/3-dependent fibroblast activation; its expression is transcriptionally regulated by JUN and epigenetically controlled via DNMT1-mediated methylation of miR-152-3p; in fetal testis, Tmsb10 transiently expressed in Leydig cell progenitors suppresses RAS/ERK signaling to drive fetal Leydig cell differentiation cooperatively with DHH and PDGF signaling.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"TMSB10 (thymosin β10) is a G-actin-binding protein that governs actin dynamics to drive cell proliferation, migration, and invasion across multiple cancers [#1, #3]. Mechanistically, TMSB10 binds G-actin and disrupts the equilibrium between G-actin-TMSB10 and G-actin-ATP interactions, controlling F-actin formation required for cell migration; its degradation via the autophagy-lysosome pathway suppresses NSCLC proliferation, migration, and invasion [#1]. In clear cell renal cell carcinoma, TMSB10 acts upstream of a PI3K/VEGF signaling axis, with knockdown reducing PI3K phosphorylation and VEGF expression [#3]. TMSB10 expression is controlled both transcriptionally, through JUN binding to its promoter [#4], and epigenetically, through DNMT1-maintained methylation of the miR-152-3p promoter that otherwise targets and suppresses TMSB10 [#2]. Beyond cancer, TMSB10 is a positive regulator of TGF-β/SMAD signaling, promoting SMAD2/3 phosphorylation and ECM accumulation in renal fibroblasts [#5], and in fetal testis it transiently marks Leydig cell progenitors where it suppresses RAS/ERK signaling to drive fetal Leydig cell differentiation [#0].\",\n  \"teleology\": [\n    {\n      \"year\": 2020,\n      \"claim\": \"Established that TMSB10 functions upstream of an oncogenic signaling axis, addressing how its expression translates into tumor cell behavior.\",\n      \"evidence\": \"TMSB10 knockdown in ccRCC cell lines with proliferation/migration/invasion assays and western blotting for PI3K phosphorylation and VEGF\",\n      \"pmids\": [\"32319572\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Single knockdown approach without reconstitution or epistasis confirmation\",\n        \"Does not establish whether PI3K/VEGF effects are direct or downstream of actin changes\",\n        \"No mechanism linking TMSB10 to PI3K activation\"\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Identified an epigenetic control circuit explaining how TMSB10 is maintained at high levels in cancer, via DNMT1/miR-152-3p.\",\n      \"evidence\": \"Methylation detection, DNMT1/miR-152-3p transfection and targeting analysis in CRC cells with in vivo tumor growth assays\",\n      \"pmids\": [\"32918845\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct binding of miR-152-3p to the TMSB10 transcript inferred from targeting analysis\",\n        \"Does not address whether this circuit operates outside colorectal cancer\"\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Defined a developmental role distinct from cancer, showing TMSB10 drives fetal Leydig cell differentiation by suppressing RAS/ERK.\",\n      \"evidence\": \"scRNA-seq identification plus functional manipulation in mouse fetal testis with RAS/ERK and PI3K/AKT pathway analysis\",\n      \"pmids\": [\"36109592\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Molecular mechanism by which TMSB10 suppresses RAS/ERK not resolved\",\n        \"Relationship between actin-binding activity and ERK suppression unclear\"\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Identified JUN as a direct transcriptional activator of TMSB10, providing an upstream determinant of its oncogenic expression.\",\n      \"evidence\": \"ChIP confirmation of JUN binding to the TMSB10 promoter with qRT-PCR and proliferation/apoptosis assays in ccRCC cells\",\n      \"pmids\": [\"35414502\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Does not establish whether JUN regulation interacts with the DNMT1/miR-152-3p axis\",\n        \"Single lab, single tumor type\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Resolved the core actin-related mechanism, showing TMSB10 binds G-actin and that its autophagic degradation disrupts F-actin formation for migration.\",\n      \"evidence\": \"GST pull-down, confocal imaging, western blotting, and TMSB10 KD/OE with proliferation/transwell assays in NSCLC; Urolithin A as a degradation inducer\",\n      \"pmids\": [\"39368341\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Structural basis of G-actin-TMSB10 binding not determined\",\n        \"Autophagy-lysosome degradation mechanism characterized only via Urolithin A treatment\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Showed the TMSB10 UTR confers high mRNA expression in antigen-presenting cells, a property exploitable for mRNA vaccine design.\",\n      \"evidence\": \"GEO mining, reporter assays in APCs/293T, and in vivo mRNA vaccine immune readouts\",\n      \"pmids\": [\"38675814\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Mechanism of high TMSB10 mRNA abundance in dendritic cells not dissected\",\n        \"Concerns the UTR element rather than TMSB10 protein function\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Extended TMSB10 function beyond cancer to fibrosis, positioning it as a positive regulator of TGF-β/SMAD2/3 signaling.\",\n      \"evidence\": \"Tmsb10 knockdown in NIH-3T3 fibroblasts and a diabetic mouse model with fibrosis marker and SMAD2/3 phosphorylation readouts; scRNA-seq for identification\",\n      \"pmids\": [\"41497884\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Mechanism linking TMSB10 to SMAD2/3 phosphorylation not defined\",\n        \"Single lab; relationship to actin-binding activity unaddressed\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Linked TMSB10 to immune microenvironment remodeling, showing it skews macrophages toward an M2 phenotype in prostate cancer.\",\n      \"evidence\": \"siRNA knockdown and overexpression in prostate cancer cell lines with co-culture macrophage polarization and cytokine assays\",\n      \"pmids\": [\"40307738\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No molecular mechanism identified for macrophage polarization\",\n        \"Co-culture readout without in vivo immune validation\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How TMSB10's single G-actin-binding activity mechanistically converges on the diverse signaling outputs (PI3K/VEGF, RAS/ERK, TGF-β/SMAD) attributed to it remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No unifying mechanism connecting actin sequestration to specific signaling cascades\",\n        \"No structural model of TMSB10 in complex with partners\",\n        \"Tissue-specific determinants of opposing roles (differentiation vs. proliferation) unknown\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [0, 3, 5]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"ACTB\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":5,"faith_total":5,"faith_pct":100.0}}