{"gene":"ST7","run_date":"2026-04-28T20:42:08","timeline":{"discoveries":[{"year":2001,"finding":"Introduction of ST7 cDNA into the prostate-cancer-derived cell line PC3 abrogated in vivo tumorigenicity in nude mice without affecting in vitro proliferation, demonstrating ST7 functions as a tumor suppressor in vivo.","method":"In vivo xenograft suppression assay with ST7 cDNA introduction into PC3 cells","journal":"Nature genetics","confidence":"High","confidence_rationale":"Tier 2 — clean gain-of-function with defined in vivo phenotypic readout, foundational paper with 75 citations","pmids":["11279520"],"is_preprint":false},{"year":2003,"finding":"ST7 protein is a member of the low-density lipoprotein receptor (LDLR) superfamily (classified as LRP12), and its cytoplasmic domain interacts with RACK1, MIBP, and SARA — proteins involved in signal transduction and/or endocytosis — as identified by yeast two-hybrid analysis.","method":"Proteomic motif analysis; yeast two-hybrid screening of ST7 cytoplasmic domain","journal":"Biochemistry","confidence":"Medium","confidence_rationale":"Tier 3 — yeast two-hybrid is a single method; interactions not confirmed by orthogonal co-IP","pmids":["12809483"],"is_preprint":false},{"year":2004,"finding":"PRMT5, associated with SWI/SNF (BRG1 and hBRM) chromatin remodeling complexes, directly methylates H3 arginine 8 (H3R8) at the ST7 promoter, leading to H3K9 deacetylation and transcriptional repression of ST7. Reduction of PRMT5 levels derepresses ST7 expression, while PRMT5 overexpression suppresses ST7 and increases cellular transformation.","method":"PRMT5 antisense knockdown, microarray, ChIP, in vitro histone methylation assay, overexpression in NIH 3T3 cells","journal":"Molecular and cellular biology","confidence":"High","confidence_rationale":"Tier 1-2 — multiple orthogonal methods (in vitro methylation assay, ChIP, KD/OE with defined phenotype), highly cited (495 citations)","pmids":["15485929"],"is_preprint":false},{"year":2006,"finding":"Re-expression of ST7 in PC-3 prostate cancer cells suppresses subcutaneous tumor growth in SCID mice and inhibits anchorage-independent colony formation in MDA-MB-231 breast cancer cells. Expression profiling revealed ST7 predominantly induces changes in extracellular matrix remodeling genes including SPARC, IGFBP5, and matrix metalloproteinases, suggesting ST7 mediates tumor suppression through modification of the tumor microenvironment.","method":"In vivo xenograft assay, soft-agar colony formation, expression profiling (microarray)","journal":"Oncogene","confidence":"Medium","confidence_rationale":"Tier 2 — multiple methods (in vivo, in vitro, transcriptomic profiling) in a single study; replicated the PC3 suppression finding","pmids":["16474848"],"is_preprint":false},{"year":2010,"finding":"ST7 protein localizes to the cytoplasm and does not translocate to the nucleus under tested conditions. Cell cycle synchronization showed ST7 and SERPINE1 are overexpressed when cells are arrested and downregulated when cells re-enter division, suggesting ST7 participates in cell cycle-regulated gene expression.","method":"Fluorescence microscopy of GFP/YFP/V5-tagged ST7 fusion proteins; cell cycle synchronization with gene expression analysis","journal":"Journal of cancer research and clinical oncology","confidence":"Medium","confidence_rationale":"Tier 2-3 — direct localization experiment with fusion proteins; cell cycle link is correlative but uses synchronization approach","pmids":["20238225"],"is_preprint":false},{"year":2019,"finding":"The CRL4DCAF4 E3 ubiquitin ligase complex (comprising CUL4A or CUL4B, DDB1, and DCAF4) specifically directs proteasomal degradation of ST7 protein. c-Myc transcriptionally activates CUL4A and CUL4B expression, thereby increasing CRL4DCAF4 activity and reducing ST7 levels to promote tumorigenesis.","method":"In vitro and in vivo ubiquitination assays; co-IP; c-Myc promoter binding (ChIP); knockdown of CUL4A/CUL4B/c-Myc with colony formation and in vivo tumor growth assays","journal":"The Journal of pathology","confidence":"High","confidence_rationale":"Tier 1-2 — in vitro and in vivo ubiquitination assays plus reciprocal co-IP and functional rescue, multiple orthogonal methods","pmids":["30945288"],"is_preprint":false},{"year":2021,"finding":"The E3 ubiquitin ligase MIB1 targets ST7 for proteasomal degradation in pancreatic cancer cells. ST7 in turn suppresses tumor growth by downregulating IQGAP1, defining a MIB1/ST7/IQGAP1 signaling axis in pancreatic cancer progression.","method":"MIB1 overexpression/knockdown, proteasomal degradation assays, in vitro and in vivo proliferation/invasion assays","journal":"Molecular oncology","confidence":"Medium","confidence_rationale":"Tier 2-3 — proteasomal degradation assay and functional rescue with defined downstream target (IQGAP1); single lab study","pmids":["33793053"],"is_preprint":false},{"year":2026,"finding":"ST7 protein binds Y-box binding protein 1 (YBX1) and blocks its nuclear translocation, thereby suppressing transcription of MMP14. ST7 silencing enhances EMT and metastatic progression in NSCLC cell lines and in a tail-vein lung metastasis mouse model.","method":"Co-IP (ST7–YBX1 interaction), nuclear translocation assay, MMP14 expression analysis, in vitro EMT assays, in vivo tail-vein metastasis model","journal":"Cellular signalling","confidence":"Medium","confidence_rationale":"Tier 2 — co-IP plus functional in vivo metastasis model; single lab study","pmids":["42025890"],"is_preprint":false}],"current_model":"ST7 is a cytoplasmic transmembrane receptor-like protein of the LDLR superfamily (LRP12) that acts as a tumor suppressor by binding partners such as YBX1 to block nuclear translocation and suppress MMP14/EMT, remodeling the extracellular matrix; its expression is epigenetically repressed by PRMT5-containing SWI/SNF complexes via H3R8 methylation, and the ST7 protein itself is subject to proteasomal degradation directed by the CRL4DCAF4 (downstream of oncogenic c-Myc) and MIB1 E3 ubiquitin ligases, with loss of ST7 promoting tumorigenicity in multiple cancer contexts."},"narrative":{"teleology":[{"year":2001,"claim":"Whether ST7 had tumor-suppressive function was unknown; introduction of ST7 cDNA into PC3 prostate cancer cells abolished xenograft tumorigenicity without affecting proliferation in vitro, establishing ST7 as a bona fide tumor suppressor acting in vivo.","evidence":"ST7 cDNA gain-of-function in PC3 cells followed by nude mouse xenograft assay","pmids":["11279520"],"confidence":"High","gaps":["Mechanism of tumor suppression uncharacterized","No downstream targets identified","Relevance beyond prostate cancer untested"]},{"year":2003,"claim":"The molecular identity of ST7 as a signaling-competent receptor and its proximal cytoplasmic partners were unknown; classification of ST7 as an LDLR superfamily member (LRP12) and identification of RACK1, MIBP, and SARA as cytoplasmic domain interactors suggested roles in signal transduction and endocytosis.","evidence":"Proteomic domain analysis and yeast two-hybrid screen of the ST7 cytoplasmic domain","pmids":["12809483"],"confidence":"Medium","gaps":["Interactions identified only by yeast two-hybrid without reciprocal co-IP validation","Functional relevance of RACK1/MIBP/SARA binding to tumor suppression not tested","Ligand for the extracellular domain unknown"]},{"year":2004,"claim":"How ST7 expression is silenced in cancer was unclear; PRMT5, in complex with SWI/SNF chromatin remodelers, was shown to methylate H3R8 at the ST7 promoter, causing H3K9 deacetylation and transcriptional repression, establishing an epigenetic mechanism for ST7 silencing.","evidence":"PRMT5 antisense knockdown, ChIP at the ST7 promoter, in vitro histone methylation assay, overexpression in NIH 3T3 cells","pmids":["15485929"],"confidence":"High","gaps":["Whether H3R8 methylation is the sole epigenetic mechanism silencing ST7 is untested","Cancer-type specificity of PRMT5-mediated repression not defined","Contributions of BRG1 vs. hBRM sub-complexes not dissected"]},{"year":2006,"claim":"The downstream effector program of ST7 tumor suppression was unknown; expression profiling upon ST7 re-expression revealed predominant changes in extracellular matrix genes (SPARC, IGFBP5, MMPs), indicating ST7 suppresses tumors by remodeling the microenvironment.","evidence":"Xenograft assay in SCID mice, soft-agar colony formation in MDA-MB-231 cells, microarray expression profiling","pmids":["16474848"],"confidence":"Medium","gaps":["Direct versus indirect transcriptional regulation not resolved","Whether ECM remodeling is necessary or sufficient for tumor suppression untested","Upstream signaling from ST7 to gene expression changes uncharacterized"]},{"year":2010,"claim":"ST7 subcellular localization and relationship to cell cycle were undefined; fluorescence imaging placed ST7 exclusively in the cytoplasm, and synchronization experiments showed ST7 is upregulated during cell cycle arrest and downregulated upon re-entry into division.","evidence":"Fluorescence microscopy of tagged ST7 fusion proteins; cell cycle synchronization with gene expression analysis","pmids":["20238225"],"confidence":"Medium","gaps":["Causal role of ST7 in cell cycle arrest versus correlation not distinguished","Whether cytoplasmic retention is regulated under specific stimuli not tested","Connection between cell cycle expression pattern and tumor suppression unclear"]},{"year":2019,"claim":"How ST7 protein levels are regulated post-translationally was unknown; the CRL4^DCAF4 E3 ubiquitin ligase complex was shown to ubiquitinate and target ST7 for proteasomal degradation, with c-Myc transcriptionally driving CUL4A/CUL4B expression to accelerate ST7 turnover and promote tumorigenesis.","evidence":"In vitro and in vivo ubiquitination assays, reciprocal co-IP, ChIP for c-Myc at CUL4 promoters, knockdown/rescue with colony formation and xenograft assays","pmids":["30945288"],"confidence":"High","gaps":["Specific degron motif on ST7 recognized by DCAF4 not mapped","Relative contributions of CUL4A versus CUL4B not resolved","Whether other substrates of CRL4^DCAF4 contribute to the tumorigenic phenotype not excluded"]},{"year":2021,"claim":"Whether additional E3 ligases regulate ST7 degradation and what effectors lie downstream of ST7 loss in pancreatic cancer were unknown; MIB1 was identified as a second E3 ligase targeting ST7 for degradation, and IQGAP1 was defined as a downstream mediator of ST7-dependent tumor suppression.","evidence":"MIB1 overexpression/knockdown, proteasomal degradation assays, in vitro and in vivo proliferation/invasion assays in pancreatic cancer cells","pmids":["33793053"],"confidence":"Medium","gaps":["Ubiquitination sites on ST7 targeted by MIB1 not mapped","Mechanism by which ST7 regulates IQGAP1 levels not defined","Whether MIB1 and CRL4^DCAF4 act redundantly or in distinct contexts not tested"]},{"year":2026,"claim":"The direct protein partner through which ST7 suppresses EMT and metastasis was unknown; ST7 was shown to bind YBX1 and block its nuclear translocation, thereby reducing MMP14 transcription and inhibiting EMT-driven metastatic progression in NSCLC.","evidence":"Co-IP of ST7–YBX1, nuclear translocation assay, MMP14 expression analysis, in vitro EMT assays, tail-vein lung metastasis model","pmids":["42025890"],"confidence":"Medium","gaps":["Structural basis of ST7–YBX1 interaction not determined","Whether YBX1 sequestration accounts for all ST7 tumor-suppressive activity not tested","Relevance of the ST7–YBX1–MMP14 axis outside NSCLC not established"]},{"year":null,"claim":"The ligand for the extracellular LDLR-related domain of ST7 and how extracellular engagement connects to cytoplasmic tumor-suppressive signaling remain unknown.","evidence":"","pmids":[],"confidence":"Low","gaps":["No extracellular ligand identified","No structural model of full-length ST7","Integration of RACK1/SARA interactions with YBX1 binding and ECM gene regulation not resolved"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[0,3,7]}],"localization":[{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[4]}],"pathway":[{"term_id":"R-HSA-1474244","term_label":"Extracellular matrix organization","supporting_discovery_ids":[3,7]}],"complexes":[],"partners":["YBX1","DCAF4","MIB1","RACK1","SARA"],"other_free_text":[]},"mechanistic_narrative":"ST7 (also classified as LRP12) is a cytoplasmic transmembrane protein of the LDLR superfamily that functions as a tumor suppressor by remodeling the extracellular matrix and restraining epithelial-to-mesenchymal transition. Re-expression of ST7 in prostate and breast cancer cells suppresses tumorigenicity in vivo and anchorage-independent growth, predominantly through transcriptional changes in extracellular matrix genes including SPARC, IGFBP5, and matrix metalloproteinases [PMID:11279520, PMID:16474848]. Mechanistically, ST7 binds the transcription/translation regulator YBX1 and prevents its nuclear translocation, thereby suppressing MMP14 transcription and EMT-driven metastasis [PMID:42025890]. ST7 expression is epigenetically repressed by PRMT5-mediated H3R8 methylation at its promoter [PMID:15485929], and ST7 protein is targeted for proteasomal degradation by both the CRL4^DCAF4 complex (transcriptionally activated by c-Myc) and the E3 ligase MIB1, linking oncogenic signaling to ST7 inactivation [PMID:30945288, PMID:33793053]."},"prefetch_data":{"uniprot":{"accession":"Q9NRC1","full_name":"Suppressor of tumorigenicity 7 protein","aliases":["Protein FAM4A1","Protein HELG"],"length_aa":585,"mass_kda":67.2,"function":"May act as a tumor suppressor","subcellular_location":"Membrane","url":"https://www.uniprot.org/uniprotkb/Q9NRC1/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/ST7","classification":"Not Classified","n_dependent_lines":5,"n_total_lines":1208,"dependency_fraction":0.0041390728476821195},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"CERS6","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/ST7","total_profiled":1310},"omim":[{"mim_id":"618299","title":"LOW DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 12; LRP12","url":"https://www.omim.org/entry/618299"},{"mim_id":"617640","title":"SUPPRESSOR OF TUMORIGENICITY 7-LIKE PROTEIN; ST7L","url":"https://www.omim.org/entry/617640"},{"mim_id":"611015","title":"AUTISM, SUSCEPTIBILITY TO, 9; AUTS9","url":"https://www.omim.org/entry/611015"},{"mim_id":"605797","title":"ANKYRIN REPEAT, SAM, AND BASIC LEUCINE ZIPPER DOMAIN-CONTAINING 1; ASZ1","url":"https://www.omim.org/entry/605797"},{"mim_id":"600833","title":"SUPPRESSOR OF TUMORIGENICITY 7; ST7","url":"https://www.omim.org/entry/600833"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Nucleoplasm","reliability":"Supported"},{"location":"Cytosol","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/ST7"},"hgnc":{"alias_symbol":["TSG7","SEN4","ETS7q","HELG","RAY1","FAM4A"],"prev_symbol":["FAM4A1"]},"alphafold":{"accession":"Q9NRC1","domains":[{"cath_id":"-","chopping":"512-552","consensus_level":"medium","plddt":76.6466,"start":512,"end":552},{"cath_id":"-","chopping":"346-509","consensus_level":"medium","plddt":88.0108,"start":346,"end":509},{"cath_id":"1.20.5","chopping":"14-51","consensus_level":"medium","plddt":75.4489,"start":14,"end":51},{"cath_id":"1.10.3450","chopping":"152-332","consensus_level":"medium","plddt":91.3561,"start":152,"end":332}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9NRC1","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9NRC1-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9NRC1-F1-predicted_aligned_error_v6.png","plddt_mean":80.38},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=ST7","jax_strain_url":"https://www.jax.org/strain/search?query=ST7"},"sequence":{"accession":"Q9NRC1","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9NRC1.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9NRC1/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9NRC1"}},"corpus_meta":[{"pmid":"15485929","id":"PMC_15485929","title":"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes.","date":"2004","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/15485929","citation_count":495,"is_preprint":false},{"pmid":"11279520","id":"PMC_11279520","title":"Mutational and functional analyses reveal that ST7 is a highly conserved tumor-suppressor gene on human chromosome 7q31.","date":"2001","source":"Nature genetics","url":"https://pubmed.ncbi.nlm.nih.gov/11279520","citation_count":75,"is_preprint":false},{"pmid":"33476649","id":"PMC_33476649","title":"p53-targeted lncRNA ST7-AS1 acts as a tumour suppressor by interacting with PTBP1 to suppress the Wnt/β-catenin signalling pathway in glioma.","date":"2021","source":"Cancer letters","url":"https://pubmed.ncbi.nlm.nih.gov/33476649","citation_count":48,"is_preprint":false},{"pmid":"12213198","id":"PMC_12213198","title":"The RAY1/ST7 tumor-suppressor locus on chromosome 7q31 represents a complex multi-transcript system.","date":"2002","source":"Genomics","url":"https://pubmed.ncbi.nlm.nih.gov/12213198","citation_count":38,"is_preprint":false},{"pmid":"12809483","id":"PMC_12809483","title":"ST7 is a novel low-density lipoprotein receptor-related protein (LRP) with a cytoplasmic tail that interacts with proteins related to signal transduction pathways.","date":"2003","source":"Biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/12809483","citation_count":35,"is_preprint":false},{"pmid":"30945288","id":"PMC_30945288","title":"Inflammation-dependent overexpression of c-Myc enhances CRL4DCAF4 E3 ligase activity and promotes ubiquitination of ST7 in colitis-associated cancer.","date":"2019","source":"The Journal of pathology","url":"https://pubmed.ncbi.nlm.nih.gov/30945288","citation_count":35,"is_preprint":false},{"pmid":"35588343","id":"PMC_35588343","title":"CAF-derived midkine promotes EMT and cisplatin resistance by upregulating lncRNA ST7-AS1 in gastric cancer.","date":"2022","source":"Molecular and cellular biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/35588343","citation_count":34,"is_preprint":false},{"pmid":"12012006","id":"PMC_12012006","title":"Molecular cloning and characterization of ST7R (ST7-like, ST7L) on human chromosome 1p13, a novel gene homologous to tumor suppressor gene ST7 on human chromosome 7q31.","date":"2002","source":"International journal of oncology","url":"https://pubmed.ncbi.nlm.nih.gov/12012006","citation_count":34,"is_preprint":false},{"pmid":"36064620","id":"PMC_36064620","title":"Infection with pathogenic Blastocystis ST7 is associated with decreased bacterial diversity and altered gut microbiome profiles in diarrheal patients.","date":"2022","source":"Parasites & vectors","url":"https://pubmed.ncbi.nlm.nih.gov/36064620","citation_count":33,"is_preprint":false},{"pmid":"30853182","id":"PMC_30853182","title":"The long noncoding RNA ST7-AS1 promotes laryngeal squamous cell 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therapy","url":"https://pubmed.ncbi.nlm.nih.gov/37469554","citation_count":0,"is_preprint":false},{"pmid":"41760777","id":"PMC_41760777","title":"Genomic analysis of a clinical Streptococcus suis ST1 isolate from CSF reveals antimicrobial resistance, virulence, and an evolutionary link to ST7.","date":"2026","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/41760777","citation_count":0,"is_preprint":false},{"pmid":"42025890","id":"PMC_42025890","title":"ST7 binds YBX1 to suppress MMP14 expression and inhibit metastasis in non-small cell lung cancer.","date":"2026","source":"Cellular signalling","url":"https://pubmed.ncbi.nlm.nih.gov/42025890","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2024.07.15.24310455","title":"<i>Blastocystis</i>in the cervix of Polish women: a subtype found in a parenteral location is different to that found in the anus","date":"2024-07-16","source":"bioRxiv","url":"https://doi.org/10.1101/2024.07.15.24310455","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":23772,"output_tokens":2043,"usd":0.05098},"stage2":{"model":"claude-opus-4-6","input_tokens":5323,"output_tokens":2382,"usd":0.129247},"total_usd":0.180227,"stage1_batch_id":"msgbatch_011rkcQdVV1RaFq9XhcG6df6","stage2_batch_id":"msgbatch_01RzgrJafdF4EWHhj5mNi6dh","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2001,\n      \"finding\": \"Introduction of ST7 cDNA into the prostate-cancer-derived cell line PC3 abrogated in vivo tumorigenicity in nude mice without affecting in vitro proliferation, demonstrating ST7 functions as a tumor suppressor in vivo.\",\n      \"method\": \"In vivo xenograft suppression assay with ST7 cDNA introduction into PC3 cells\",\n      \"journal\": \"Nature genetics\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — clean gain-of-function with defined in vivo phenotypic readout, foundational paper with 75 citations\",\n      \"pmids\": [\"11279520\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2003,\n      \"finding\": \"ST7 protein is a member of the low-density lipoprotein receptor (LDLR) superfamily (classified as LRP12), and its cytoplasmic domain interacts with RACK1, MIBP, and SARA — proteins involved in signal transduction and/or endocytosis — as identified by yeast two-hybrid analysis.\",\n      \"method\": \"Proteomic motif analysis; yeast two-hybrid screening of ST7 cytoplasmic domain\",\n      \"journal\": \"Biochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 — yeast two-hybrid is a single method; interactions not confirmed by orthogonal co-IP\",\n      \"pmids\": [\"12809483\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2004,\n      \"finding\": \"PRMT5, associated with SWI/SNF (BRG1 and hBRM) chromatin remodeling complexes, directly methylates H3 arginine 8 (H3R8) at the ST7 promoter, leading to H3K9 deacetylation and transcriptional repression of ST7. Reduction of PRMT5 levels derepresses ST7 expression, while PRMT5 overexpression suppresses ST7 and increases cellular transformation.\",\n      \"method\": \"PRMT5 antisense knockdown, microarray, ChIP, in vitro histone methylation assay, overexpression in NIH 3T3 cells\",\n      \"journal\": \"Molecular and cellular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 — multiple orthogonal methods (in vitro methylation assay, ChIP, KD/OE with defined phenotype), highly cited (495 citations)\",\n      \"pmids\": [\"15485929\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2006,\n      \"finding\": \"Re-expression of ST7 in PC-3 prostate cancer cells suppresses subcutaneous tumor growth in SCID mice and inhibits anchorage-independent colony formation in MDA-MB-231 breast cancer cells. Expression profiling revealed ST7 predominantly induces changes in extracellular matrix remodeling genes including SPARC, IGFBP5, and matrix metalloproteinases, suggesting ST7 mediates tumor suppression through modification of the tumor microenvironment.\",\n      \"method\": \"In vivo xenograft assay, soft-agar colony formation, expression profiling (microarray)\",\n      \"journal\": \"Oncogene\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — multiple methods (in vivo, in vitro, transcriptomic profiling) in a single study; replicated the PC3 suppression finding\",\n      \"pmids\": [\"16474848\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"ST7 protein localizes to the cytoplasm and does not translocate to the nucleus under tested conditions. Cell cycle synchronization showed ST7 and SERPINE1 are overexpressed when cells are arrested and downregulated when cells re-enter division, suggesting ST7 participates in cell cycle-regulated gene expression.\",\n      \"method\": \"Fluorescence microscopy of GFP/YFP/V5-tagged ST7 fusion proteins; cell cycle synchronization with gene expression analysis\",\n      \"journal\": \"Journal of cancer research and clinical oncology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 — direct localization experiment with fusion proteins; cell cycle link is correlative but uses synchronization approach\",\n      \"pmids\": [\"20238225\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"The CRL4DCAF4 E3 ubiquitin ligase complex (comprising CUL4A or CUL4B, DDB1, and DCAF4) specifically directs proteasomal degradation of ST7 protein. c-Myc transcriptionally activates CUL4A and CUL4B expression, thereby increasing CRL4DCAF4 activity and reducing ST7 levels to promote tumorigenesis.\",\n      \"method\": \"In vitro and in vivo ubiquitination assays; co-IP; c-Myc promoter binding (ChIP); knockdown of CUL4A/CUL4B/c-Myc with colony formation and in vivo tumor growth assays\",\n      \"journal\": \"The Journal of pathology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 — in vitro and in vivo ubiquitination assays plus reciprocal co-IP and functional rescue, multiple orthogonal methods\",\n      \"pmids\": [\"30945288\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"The E3 ubiquitin ligase MIB1 targets ST7 for proteasomal degradation in pancreatic cancer cells. ST7 in turn suppresses tumor growth by downregulating IQGAP1, defining a MIB1/ST7/IQGAP1 signaling axis in pancreatic cancer progression.\",\n      \"method\": \"MIB1 overexpression/knockdown, proteasomal degradation assays, in vitro and in vivo proliferation/invasion assays\",\n      \"journal\": \"Molecular oncology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 — proteasomal degradation assay and functional rescue with defined downstream target (IQGAP1); single lab study\",\n      \"pmids\": [\"33793053\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"ST7 protein binds Y-box binding protein 1 (YBX1) and blocks its nuclear translocation, thereby suppressing transcription of MMP14. ST7 silencing enhances EMT and metastatic progression in NSCLC cell lines and in a tail-vein lung metastasis mouse model.\",\n      \"method\": \"Co-IP (ST7–YBX1 interaction), nuclear translocation assay, MMP14 expression analysis, in vitro EMT assays, in vivo tail-vein metastasis model\",\n      \"journal\": \"Cellular signalling\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — co-IP plus functional in vivo metastasis model; single lab study\",\n      \"pmids\": [\"42025890\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"ST7 is a cytoplasmic transmembrane receptor-like protein of the LDLR superfamily (LRP12) that acts as a tumor suppressor by binding partners such as YBX1 to block nuclear translocation and suppress MMP14/EMT, remodeling the extracellular matrix; its expression is epigenetically repressed by PRMT5-containing SWI/SNF complexes via H3R8 methylation, and the ST7 protein itself is subject to proteasomal degradation directed by the CRL4DCAF4 (downstream of oncogenic c-Myc) and MIB1 E3 ubiquitin ligases, with loss of ST7 promoting tumorigenicity in multiple cancer contexts.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"ST7 (also classified as LRP12) is a cytoplasmic transmembrane protein of the LDLR superfamily that functions as a tumor suppressor by remodeling the extracellular matrix and restraining epithelial-to-mesenchymal transition. Re-expression of ST7 in prostate and breast cancer cells suppresses tumorigenicity in vivo and anchorage-independent growth, predominantly through transcriptional changes in extracellular matrix genes including SPARC, IGFBP5, and matrix metalloproteinases [PMID:11279520, PMID:16474848]. Mechanistically, ST7 binds the transcription/translation regulator YBX1 and prevents its nuclear translocation, thereby suppressing MMP14 transcription and EMT-driven metastasis [PMID:42025890]. ST7 expression is epigenetically repressed by PRMT5-mediated H3R8 methylation at its promoter [PMID:15485929], and ST7 protein is targeted for proteasomal degradation by both the CRL4^DCAF4 complex (transcriptionally activated by c-Myc) and the E3 ligase MIB1, linking oncogenic signaling to ST7 inactivation [PMID:30945288, PMID:33793053].\",\n  \"teleology\": [\n    {\n      \"year\": 2001,\n      \"claim\": \"Whether ST7 had tumor-suppressive function was unknown; introduction of ST7 cDNA into PC3 prostate cancer cells abolished xenograft tumorigenicity without affecting proliferation in vitro, establishing ST7 as a bona fide tumor suppressor acting in vivo.\",\n      \"evidence\": \"ST7 cDNA gain-of-function in PC3 cells followed by nude mouse xenograft assay\",\n      \"pmids\": [\"11279520\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Mechanism of tumor suppression uncharacterized\", \"No downstream targets identified\", \"Relevance beyond prostate cancer untested\"]\n    },\n    {\n      \"year\": 2003,\n      \"claim\": \"The molecular identity of ST7 as a signaling-competent receptor and its proximal cytoplasmic partners were unknown; classification of ST7 as an LDLR superfamily member (LRP12) and identification of RACK1, MIBP, and SARA as cytoplasmic domain interactors suggested roles in signal transduction and endocytosis.\",\n      \"evidence\": \"Proteomic domain analysis and yeast two-hybrid screen of the ST7 cytoplasmic domain\",\n      \"pmids\": [\"12809483\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Interactions identified only by yeast two-hybrid without reciprocal co-IP validation\", \"Functional relevance of RACK1/MIBP/SARA binding to tumor suppression not tested\", \"Ligand for the extracellular domain unknown\"]\n    },\n    {\n      \"year\": 2004,\n      \"claim\": \"How ST7 expression is silenced in cancer was unclear; PRMT5, in complex with SWI/SNF chromatin remodelers, was shown to methylate H3R8 at the ST7 promoter, causing H3K9 deacetylation and transcriptional repression, establishing an epigenetic mechanism for ST7 silencing.\",\n      \"evidence\": \"PRMT5 antisense knockdown, ChIP at the ST7 promoter, in vitro histone methylation assay, overexpression in NIH 3T3 cells\",\n      \"pmids\": [\"15485929\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether H3R8 methylation is the sole epigenetic mechanism silencing ST7 is untested\", \"Cancer-type specificity of PRMT5-mediated repression not defined\", \"Contributions of BRG1 vs. hBRM sub-complexes not dissected\"]\n    },\n    {\n      \"year\": 2006,\n      \"claim\": \"The downstream effector program of ST7 tumor suppression was unknown; expression profiling upon ST7 re-expression revealed predominant changes in extracellular matrix genes (SPARC, IGFBP5, MMPs), indicating ST7 suppresses tumors by remodeling the microenvironment.\",\n      \"evidence\": \"Xenograft assay in SCID mice, soft-agar colony formation in MDA-MB-231 cells, microarray expression profiling\",\n      \"pmids\": [\"16474848\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct versus indirect transcriptional regulation not resolved\", \"Whether ECM remodeling is necessary or sufficient for tumor suppression untested\", \"Upstream signaling from ST7 to gene expression changes uncharacterized\"]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"ST7 subcellular localization and relationship to cell cycle were undefined; fluorescence imaging placed ST7 exclusively in the cytoplasm, and synchronization experiments showed ST7 is upregulated during cell cycle arrest and downregulated upon re-entry into division.\",\n      \"evidence\": \"Fluorescence microscopy of tagged ST7 fusion proteins; cell cycle synchronization with gene expression analysis\",\n      \"pmids\": [\"20238225\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Causal role of ST7 in cell cycle arrest versus correlation not distinguished\", \"Whether cytoplasmic retention is regulated under specific stimuli not tested\", \"Connection between cell cycle expression pattern and tumor suppression unclear\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"How ST7 protein levels are regulated post-translationally was unknown; the CRL4^DCAF4 E3 ubiquitin ligase complex was shown to ubiquitinate and target ST7 for proteasomal degradation, with c-Myc transcriptionally driving CUL4A/CUL4B expression to accelerate ST7 turnover and promote tumorigenesis.\",\n      \"evidence\": \"In vitro and in vivo ubiquitination assays, reciprocal co-IP, ChIP for c-Myc at CUL4 promoters, knockdown/rescue with colony formation and xenograft assays\",\n      \"pmids\": [\"30945288\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Specific degron motif on ST7 recognized by DCAF4 not mapped\", \"Relative contributions of CUL4A versus CUL4B not resolved\", \"Whether other substrates of CRL4^DCAF4 contribute to the tumorigenic phenotype not excluded\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Whether additional E3 ligases regulate ST7 degradation and what effectors lie downstream of ST7 loss in pancreatic cancer were unknown; MIB1 was identified as a second E3 ligase targeting ST7 for degradation, and IQGAP1 was defined as a downstream mediator of ST7-dependent tumor suppression.\",\n      \"evidence\": \"MIB1 overexpression/knockdown, proteasomal degradation assays, in vitro and in vivo proliferation/invasion assays in pancreatic cancer cells\",\n      \"pmids\": [\"33793053\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Ubiquitination sites on ST7 targeted by MIB1 not mapped\", \"Mechanism by which ST7 regulates IQGAP1 levels not defined\", \"Whether MIB1 and CRL4^DCAF4 act redundantly or in distinct contexts not tested\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"The direct protein partner through which ST7 suppresses EMT and metastasis was unknown; ST7 was shown to bind YBX1 and block its nuclear translocation, thereby reducing MMP14 transcription and inhibiting EMT-driven metastatic progression in NSCLC.\",\n      \"evidence\": \"Co-IP of ST7–YBX1, nuclear translocation assay, MMP14 expression analysis, in vitro EMT assays, tail-vein lung metastasis model\",\n      \"pmids\": [\"42025890\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Structural basis of ST7–YBX1 interaction not determined\", \"Whether YBX1 sequestration accounts for all ST7 tumor-suppressive activity not tested\", \"Relevance of the ST7–YBX1–MMP14 axis outside NSCLC not established\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The ligand for the extracellular LDLR-related domain of ST7 and how extracellular engagement connects to cytoplasmic tumor-suppressive signaling remain unknown.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No extracellular ligand identified\", \"No structural model of full-length ST7\", \"Integration of RACK1/SARA interactions with YBX1 binding and ECM gene regulation not resolved\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [0, 3, 7]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [4]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1474244\", \"supporting_discovery_ids\": [3, 7]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"YBX1\", \"DCAF4\", \"MIB1\", \"RACK1\", \"SARA\"],\n    \"other_free_text\": []\n  }\n}\n```"}