{"gene":"BET1","run_date":"2026-04-28T17:12:38","timeline":{"discoveries":[{"year":1990,"finding":"BET1 is required for vesicular transport from the endoplasmic reticulum to the Golgi complex in S. cerevisiae; genetic epistasis shows BET1 interacts with BOS1 and SEC22, and a bet1 sec22 double mutant is inviable, placing BET1 in the ER-to-Golgi transport pathway","method":"Genetic complementation, multicopy suppression, double-mutant lethality analysis in yeast","journal":"Molecular and cellular biology","confidence":"High","confidence_rationale":"Tier 2 — genetic epistasis replicated across multiple gene pairs, foundational study with 160 citations","pmids":["2192256"],"is_preprint":false},{"year":2001,"finding":"Mammalian Bet1 forms a SNARE complex with Ykt6, syntaxin 5, and GS28, and this complex functions in a late stage of ER-to-Golgi transport","method":"Co-immunoprecipitation, in vitro ER-Golgi transport assay with inhibitory antibodies, microinjection of Ykt6 antibodies","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 — reciprocal Co-IP combined with functional in vitro transport inhibition assay, 113 citations","pmids":["11323436"],"is_preprint":false},{"year":2019,"finding":"MT1-MMP recruits Bet1 away from its canonical ER-Golgi SNARE function; in invasive cancer cells Bet1 localizes to MT1-MMP-positive endosomes and forms a novel SNARE complex with syntaxin 4 and endosomal SNAREs to promote MT1-MMP trafficking to the cell surface/invadopodia; Bet1 also facilitates MT1-MMP exit from raft-like ER structures","method":"Co-immunoprecipitation, fluorescence co-localization, knockdown with trafficking phenotype readout","journal":"The Journal of cell biology","confidence":"Medium","confidence_rationale":"Tier 2/3 — multiple orthogonal methods in single study but not independently replicated","pmids":["31519727"],"is_preprint":false},{"year":2021,"finding":"BET1, together with SNARE complex partners GOSR2, SEC22b, and Syntaxin-5, is required for fusion of ER-derived vesicles with the ERGIC and cis-Golgi; loss-of-function variants impair ER-to-Golgi transport and mislocalize ERGIC-53; BET1 physically interacts with ERGIC-53 as validated by endogenous co-immunoprecipitation and co-localization at the ERGIC compartment","method":"Endogenous co-immunoprecipitation, co-localization by immunofluorescence, in silico structural modeling, analysis of patient-derived fibroblasts with BET1 loss-of-function variants","journal":"EMBO molecular medicine","confidence":"High","confidence_rationale":"Tier 2 — endogenous Co-IP with co-localization, functional validation using patient variants and fibroblast assays","pmids":["34779586"],"is_preprint":false}],"current_model":"BET1 is a SNARE protein that forms a complex with GOSR2/GS28, SEC22b, and Syntaxin-5 to mediate fusion of ER-derived vesicles with the ERGIC and cis-Golgi; it also interacts with ERGIC-53 at the ERGIC compartment, and in invasive cells can be recruited by MT1-MMP into endosomal SNARE complexes containing syntaxin 4 to promote trafficking to the plasma membrane/invadopodia."},"narrative":{"teleology":[{"year":1990,"claim":"Establishing BET1 as a component of ER-to-Golgi transport resolved its pathway placement: genetic epistasis in yeast showed BET1 interacts functionally with BOS1 and SEC22, and double-mutant lethality confirmed a non-redundant role in vesicular traffic from the ER.","evidence":"Genetic complementation, multicopy suppression, and double-mutant lethality analysis in S. cerevisiae","pmids":["2192256"],"confidence":"High","gaps":["Biochemical mechanism of BET1 action (e.g., SNARE complex composition) not yet defined","Mammalian homolog function not addressed"]},{"year":2001,"claim":"Identifying the mammalian BET1-containing SNARE complex (with Ykt6, syntaxin 5, and GS28) and showing that disrupting it blocks a late stage of ER-to-Golgi transport established the biochemical basis for BET1's fusogenic role.","evidence":"Reciprocal co-immunoprecipitation and in vitro ER-Golgi transport assay with inhibitory antibodies in mammalian cells","pmids":["11323436"],"confidence":"High","gaps":["Identity of the target membrane (ERGIC vs. cis-Golgi) not distinguished","No structural information on the assembled SNARE complex"]},{"year":2019,"claim":"Discovering that MT1-MMP redirects BET1 to endosomal SNARE complexes containing syntaxin 4 revealed a non-canonical trafficking role for BET1 in invasive cells, linking SNARE reprogramming to invadopodia formation.","evidence":"Co-immunoprecipitation, fluorescence co-localization, and knockdown with trafficking phenotype readout in invasive cancer cell lines","pmids":["31519727"],"confidence":"Medium","gaps":["Not independently replicated in a second study or laboratory","Structural basis for MT1-MMP-dependent BET1 recruitment unknown","Generality across cancer types not tested"]},{"year":2021,"claim":"Demonstrating that BET1 loss-of-function variants impair ER-to-Golgi transport and mislocalize ERGIC-53, combined with endogenous co-immunoprecipitation of BET1 with ERGIC-53, pinpointed BET1's fusogenic activity to the ERGIC compartment and linked it to human disease.","evidence":"Endogenous co-immunoprecipitation, immunofluorescence co-localization, and functional analysis of patient-derived fibroblasts with BET1 loss-of-function variants","pmids":["34779586"],"confidence":"High","gaps":["Structural model of BET1–ERGIC-53 interaction not experimentally validated","Relative contributions of BET1 vs. BET1L at the ERGIC remain unresolved"]},{"year":null,"claim":"How BET1 is selectively incorporated into canonical versus non-canonical SNARE complexes (e.g., syntaxin-5 vs. syntaxin-4 containing), and what regulatory signals control this partitioning, remain unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No structural data for any BET1-containing SNARE complex","Regulatory post-translational modifications on BET1 not characterized","In vivo phenotype of complete BET1 loss in mammalian models not fully described"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[0,1,3]}],"localization":[{"term_id":"GO:0005783","term_label":"endoplasmic reticulum","supporting_discovery_ids":[0,2,3]},{"term_id":"GO:0005794","term_label":"Golgi apparatus","supporting_discovery_ids":[0,1,3]},{"term_id":"GO:0005768","term_label":"endosome","supporting_discovery_ids":[2]},{"term_id":"GO:0031410","term_label":"cytoplasmic vesicle","supporting_discovery_ids":[0,1,3]}],"pathway":[{"term_id":"R-HSA-5653656","term_label":"Vesicle-mediated transport","supporting_discovery_ids":[0,1,3]},{"term_id":"R-HSA-9609507","term_label":"Protein localization","supporting_discovery_ids":[0,1,2,3]}],"complexes":["BET1–Syntaxin-5–GS28–SEC22b SNARE complex"],"partners":["STX5","GOSR2","SEC22B","YKT6","LMAN1","STX4","MMP14"],"other_free_text":[]},"mechanistic_narrative":"BET1 is a SNARE protein essential for vesicular transport from the endoplasmic reticulum to the Golgi complex. It forms a SNARE complex with GOSR2/GS28, SEC22b, and Syntaxin-5 to mediate fusion of ER-derived vesicles with the ERGIC and cis-Golgi, and it physically interacts with the cargo receptor ERGIC-53 at the ERGIC compartment; loss-of-function variants impair ER-to-Golgi transport and mislocalize ERGIC-53 [PMID:2192256, PMID:11323436, PMID:34779586]. In invasive cancer cells, MT1-MMP redirects BET1 from its canonical ER-Golgi role to endosomal compartments, where BET1 assembles a non-canonical SNARE complex with syntaxin 4 to promote MT1-MMP trafficking to invadopodia [PMID:31519727]."},"prefetch_data":{"uniprot":{"accession":"O15155","full_name":"BET1 homolog","aliases":["Golgi vesicular membrane-trafficking protein p18"],"length_aa":118,"mass_kda":13.3,"function":"Required for vesicular transport from the ER to the Golgi complex (PubMed:34779586). Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane (By similarity)","subcellular_location":"Endoplasmic reticulum membrane; Golgi apparatus, cis-Golgi network membrane; Golgi apparatus membrane","url":"https://www.uniprot.org/uniprotkb/O15155/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/BET1","classification":"Common Essential","n_dependent_lines":428,"n_total_lines":1208,"dependency_fraction":0.3543046357615894},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000105829","cell_line_id":"CID000746","localizations":[{"compartment":"vesicles","grade":3}],"interactors":[{"gene":"BET1;DKFZP781C0425","stoichiometry":10.0},{"gene":"NSF","stoichiometry":4.0},{"gene":"NAPA","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/target/CID000746","total_profiled":1310},"omim":[{"mim_id":"615417","title":"BET1-LIKE PROTEIN; BET1L","url":"https://www.omim.org/entry/615417"},{"mim_id":"612442","title":"SEC22 HOMOLOG A, VESICLE TRAFFICKING PROTEIN; SEC22A","url":"https://www.omim.org/entry/612442"},{"mim_id":"605456","title":"BET1 GOLGI VESICULAR MEMBRANE-TRAFFICKING PROTEIN; BET1","url":"https://www.omim.org/entry/605456"},{"mim_id":"604029","title":"SEC22 HOMOLOG B, VESICLE TRAFFICKING PROTEIN; SEC22B","url":"https://www.omim.org/entry/604029"},{"mim_id":"604028","title":"SEC22 HOMOLOG C, VESICLE TRAFFICKING PROTEIN; SEC22C","url":"https://www.omim.org/entry/604028"}],"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/BET1"},"hgnc":{"alias_symbol":["hbet1"],"prev_symbol":[]},"alphafold":{"accession":"O15155","domains":[{"cath_id":"1.20.5","chopping":"22-91","consensus_level":"high","plddt":90.8877,"start":22,"end":91}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O15155","model_url":"https://alphafold.ebi.ac.uk/files/AF-O15155-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O15155-F1-predicted_aligned_error_v6.png","plddt_mean":83.06},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=BET1","jax_strain_url":"https://www.jax.org/strain/search?query=BET1"},"sequence":{"accession":"O15155","fasta_url":"https://rest.uniprot.org/uniprotkb/O15155.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O15155/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O15155"}},"corpus_meta":[{"pmid":"2192256","id":"PMC_2192256","title":"BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex.","date":"1990","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/2192256","citation_count":160,"is_preprint":false},{"pmid":"11323436","id":"PMC_11323436","title":"Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport.","date":"2001","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/11323436","citation_count":113,"is_preprint":false},{"pmid":"7647565","id":"PMC_7647565","title":"Molecular characterization of BET1, a gene expressed in the endosperm transfer cells of maize.","date":"1995","source":"The Plant cell","url":"https://pubmed.ncbi.nlm.nih.gov/7647565","citation_count":71,"is_preprint":false},{"pmid":"20181741","id":"PMC_20181741","title":"Double bromodomain protein BET-1 and MYST HATs establish and maintain stable cell fates in C. elegans.","date":"2010","source":"Development (Cambridge, England)","url":"https://pubmed.ncbi.nlm.nih.gov/20181741","citation_count":21,"is_preprint":false},{"pmid":"31519727","id":"PMC_31519727","title":"MT1-MMP recruits the ER-Golgi SNARE Bet1 for efficient MT1-MMP transport to the plasma membrane.","date":"2019","source":"The Journal of cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/31519727","citation_count":19,"is_preprint":false},{"pmid":"11445081","id":"PMC_11445081","title":"AtBS14a and AtBS14b, two Bet1/Sft1-like SNAREs from Arabidopsis thaliana that complement mutations in the yeast SFT1 gene.","date":"2001","source":"FEBS letters","url":"https://pubmed.ncbi.nlm.nih.gov/11445081","citation_count":18,"is_preprint":false},{"pmid":"34779586","id":"PMC_34779586","title":"BET1 variants establish impaired vesicular transport as a cause for muscular dystrophy with epilepsy.","date":"2021","source":"EMBO molecular medicine","url":"https://pubmed.ncbi.nlm.nih.gov/34779586","citation_count":14,"is_preprint":false},{"pmid":"36404134","id":"PMC_36404134","title":"Large-scale genetic screens identify BET-1 as a cytoskeleton regulator promoting actin function and life span.","date":"2022","source":"Aging cell","url":"https://pubmed.ncbi.nlm.nih.gov/36404134","citation_count":13,"is_preprint":false},{"pmid":"24285704","id":"PMC_24285704","title":"Maintenance of muscle myosin levels in adult C. elegans requires both the double bromodomain protein BET-1 and sumoylation.","date":"2013","source":"Biology open","url":"https://pubmed.ncbi.nlm.nih.gov/24285704","citation_count":7,"is_preprint":false},{"pmid":"24349540","id":"PMC_24349540","title":"An RNAi-based dimorphic genetic screen identified the double bromodomain protein BET-1 as a sumo-dependent attenuator of RAS-mediated signalling.","date":"2013","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/24349540","citation_count":2,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5934,"output_tokens":1065,"usd":0.016889},"stage2":{"model":"claude-opus-4-6","input_tokens":4263,"output_tokens":1618,"usd":0.092647},"total_usd":0.109536,"stage1_batch_id":"msgbatch_01TqNM6p6FsoMBT2jzQTwKBr","stage2_batch_id":"msgbatch_01Ya473eco8sTHbvRymQaU8o","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1990,\n      \"finding\": \"BET1 is required for vesicular transport from the endoplasmic reticulum to the Golgi complex in S. cerevisiae; genetic epistasis shows BET1 interacts with BOS1 and SEC22, and a bet1 sec22 double mutant is inviable, placing BET1 in the ER-to-Golgi transport pathway\",\n      \"method\": \"Genetic complementation, multicopy suppression, double-mutant lethality analysis in yeast\",\n      \"journal\": \"Molecular and cellular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — genetic epistasis replicated across multiple gene pairs, foundational study with 160 citations\",\n      \"pmids\": [\"2192256\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2001,\n      \"finding\": \"Mammalian Bet1 forms a SNARE complex with Ykt6, syntaxin 5, and GS28, and this complex functions in a late stage of ER-to-Golgi transport\",\n      \"method\": \"Co-immunoprecipitation, in vitro ER-Golgi transport assay with inhibitory antibodies, microinjection of Ykt6 antibodies\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — reciprocal Co-IP combined with functional in vitro transport inhibition assay, 113 citations\",\n      \"pmids\": [\"11323436\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"MT1-MMP recruits Bet1 away from its canonical ER-Golgi SNARE function; in invasive cancer cells Bet1 localizes to MT1-MMP-positive endosomes and forms a novel SNARE complex with syntaxin 4 and endosomal SNAREs to promote MT1-MMP trafficking to the cell surface/invadopodia; Bet1 also facilitates MT1-MMP exit from raft-like ER structures\",\n      \"method\": \"Co-immunoprecipitation, fluorescence co-localization, knockdown with trafficking phenotype readout\",\n      \"journal\": \"The Journal of cell biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2/3 — multiple orthogonal methods in single study but not independently replicated\",\n      \"pmids\": [\"31519727\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"BET1, together with SNARE complex partners GOSR2, SEC22b, and Syntaxin-5, is required for fusion of ER-derived vesicles with the ERGIC and cis-Golgi; loss-of-function variants impair ER-to-Golgi transport and mislocalize ERGIC-53; BET1 physically interacts with ERGIC-53 as validated by endogenous co-immunoprecipitation and co-localization at the ERGIC compartment\",\n      \"method\": \"Endogenous co-immunoprecipitation, co-localization by immunofluorescence, in silico structural modeling, analysis of patient-derived fibroblasts with BET1 loss-of-function variants\",\n      \"journal\": \"EMBO molecular medicine\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — endogenous Co-IP with co-localization, functional validation using patient variants and fibroblast assays\",\n      \"pmids\": [\"34779586\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"BET1 is a SNARE protein that forms a complex with GOSR2/GS28, SEC22b, and Syntaxin-5 to mediate fusion of ER-derived vesicles with the ERGIC and cis-Golgi; it also interacts with ERGIC-53 at the ERGIC compartment, and in invasive cells can be recruited by MT1-MMP into endosomal SNARE complexes containing syntaxin 4 to promote trafficking to the plasma membrane/invadopodia.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"BET1 is a SNARE protein essential for vesicular transport from the endoplasmic reticulum to the Golgi complex. It forms a SNARE complex with GOSR2/GS28, SEC22b, and Syntaxin-5 to mediate fusion of ER-derived vesicles with the ERGIC and cis-Golgi, and it physically interacts with the cargo receptor ERGIC-53 at the ERGIC compartment; loss-of-function variants impair ER-to-Golgi transport and mislocalize ERGIC-53 [PMID:2192256, PMID:11323436, PMID:34779586]. In invasive cancer cells, MT1-MMP redirects BET1 from its canonical ER-Golgi role to endosomal compartments, where BET1 assembles a non-canonical SNARE complex with syntaxin 4 to promote MT1-MMP trafficking to invadopodia [PMID:31519727].\",\n  \"teleology\": [\n    {\n      \"year\": 1990,\n      \"claim\": \"Establishing BET1 as a component of ER-to-Golgi transport resolved its pathway placement: genetic epistasis in yeast showed BET1 interacts functionally with BOS1 and SEC22, and double-mutant lethality confirmed a non-redundant role in vesicular traffic from the ER.\",\n      \"evidence\": \"Genetic complementation, multicopy suppression, and double-mutant lethality analysis in S. cerevisiae\",\n      \"pmids\": [\"2192256\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Biochemical mechanism of BET1 action (e.g., SNARE complex composition) not yet defined\",\n        \"Mammalian homolog function not addressed\"\n      ]\n    },\n    {\n      \"year\": 2001,\n      \"claim\": \"Identifying the mammalian BET1-containing SNARE complex (with Ykt6, syntaxin 5, and GS28) and showing that disrupting it blocks a late stage of ER-to-Golgi transport established the biochemical basis for BET1's fusogenic role.\",\n      \"evidence\": \"Reciprocal co-immunoprecipitation and in vitro ER-Golgi transport assay with inhibitory antibodies in mammalian cells\",\n      \"pmids\": [\"11323436\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Identity of the target membrane (ERGIC vs. cis-Golgi) not distinguished\",\n        \"No structural information on the assembled SNARE complex\"\n      ]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Discovering that MT1-MMP redirects BET1 to endosomal SNARE complexes containing syntaxin 4 revealed a non-canonical trafficking role for BET1 in invasive cells, linking SNARE reprogramming to invadopodia formation.\",\n      \"evidence\": \"Co-immunoprecipitation, fluorescence co-localization, and knockdown with trafficking phenotype readout in invasive cancer cell lines\",\n      \"pmids\": [\"31519727\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Not independently replicated in a second study or laboratory\",\n        \"Structural basis for MT1-MMP-dependent BET1 recruitment unknown\",\n        \"Generality across cancer types not tested\"\n      ]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Demonstrating that BET1 loss-of-function variants impair ER-to-Golgi transport and mislocalize ERGIC-53, combined with endogenous co-immunoprecipitation of BET1 with ERGIC-53, pinpointed BET1's fusogenic activity to the ERGIC compartment and linked it to human disease.\",\n      \"evidence\": \"Endogenous co-immunoprecipitation, immunofluorescence co-localization, and functional analysis of patient-derived fibroblasts with BET1 loss-of-function variants\",\n      \"pmids\": [\"34779586\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural model of BET1–ERGIC-53 interaction not experimentally validated\",\n        \"Relative contributions of BET1 vs. BET1L at the ERGIC remain unresolved\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How BET1 is selectively incorporated into canonical versus non-canonical SNARE complexes (e.g., syntaxin-5 vs. syntaxin-4 containing), and what regulatory signals control this partitioning, remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No structural data for any BET1-containing SNARE complex\",\n        \"Regulatory post-translational modifications on BET1 not characterized\",\n        \"In vivo phenotype of complete BET1 loss in mammalian models not fully described\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [0, 1, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005783\", \"supporting_discovery_ids\": [0, 2, 3]},\n      {\"term_id\": \"GO:0005794\", \"supporting_discovery_ids\": [0, 1, 3]},\n      {\"term_id\": \"GO:0005768\", \"supporting_discovery_ids\": [2]},\n      {\"term_id\": \"GO:0031410\", \"supporting_discovery_ids\": [0, 1, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-5653656\", \"supporting_discovery_ids\": [0, 1, 3]},\n      {\"term_id\": \"R-HSA-9609507\", \"supporting_discovery_ids\": [0, 1, 2, 3]}\n    ],\n    \"complexes\": [\n      \"BET1–Syntaxin-5–GS28–SEC22b SNARE complex\"\n    ],\n    \"partners\": [\n      \"STX5\",\n      \"GOSR2\",\n      \"SEC22B\",\n      \"YKT6\",\n      \"LMAN1\",\n      \"STX4\",\n      \"MMP14\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```"}