{"gene":"STX10","run_date":"2026-06-10T10:51:54","timeline":{"discoveries":[{"year":1998,"finding":"STX10 (hsyn10) was cloned as a new syntaxin family member and localized to the trans-Golgi network by indirect immunofluorescence, with colocalization with the Golgi SNARE GS28; brefeldin A (but not wortmannin) treatment disrupted its staining pattern, confirming TGN localization.","method":"Indirect immunofluorescence, subcellular fractionation/colocalization with Golgi markers, brefeldin A and wortmannin pharmacological perturbation","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization experiment with pharmacological validation, single lab, two orthogonal perturbation methods","pmids":["9446797"],"is_preprint":false},{"year":2008,"finding":"STX10 forms a SNARE complex with STX16, Vti1a, and VAMP3 that is specifically required for retrograde transport of mannose 6-phosphate receptors (MPRs) from endosomes to the trans-Golgi network; depletion of STX10 causes MPR missorting and hypersecretion of hexosaminidase. This STX10-dependent route is distinct from the STX6-dependent route used by TGN46 and cholera toxin. Mouse and rat cells lack STX10 and must use a different t-SNARE for this process. Additionally, the tether GCC185 binds directly to STX16 and this interaction is competed by Rab6, supporting a model in which GCC185 helps Rab9-bearing vesicles deliver cargo to the trans-Golgi.","method":"siRNA depletion, co-immunoprecipitation, hexosaminidase secretion assay, MPR trafficking assay, direct binding assay (GCC185–STX16), Rab6 competition assay","journal":"The Journal of cell biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP, functional rescue, multiple orthogonal assays (secretion, trafficking, direct binding), replicated across multiple cell lines including mouse/rat lacking STX10","pmids":["18195106"],"is_preprint":false},{"year":2021,"finding":"Using BioID proximity labeling, a novel protein-protein interaction between STX10 and VAPB was identified. However, addition of the BirA* tag altered STX10 localization during Chlamydia trachomatis and Coxiella burnetii infection, indicating the fusion construct is not reliable for studying STX10 trafficking dynamics during intracellular pathogen infection.","method":"BioID proximity labeling, fluorescence microscopy of BirA*-Stx10 fusion constructs during infection","journal":"Pathogens and disease","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single proximity-labeling experiment, single lab, no validation of the STX10–VAPB interaction by orthogonal method","pmids":["34323972"],"is_preprint":false}],"current_model":"STX10 is a trans-Golgi network-localized t-SNARE that assembles into a quaternary SNARE complex with STX16, Vti1a, and VAMP3 to mediate the specific retrograde transport of mannose 6-phosphate receptors from late endosomes to the trans-Golgi network, a route distinct from the STX6-dependent pathway used by TGN46; the tether GCC185 facilitates this process by binding STX16 in a Rab6-regulated manner, and STX10 has also been found to interact with VAPB by proximity labeling."},"narrative":{"mechanistic_narrative":"STX10 is a trans-Golgi network (TGN)-localized t-SNARE that mediates the specific retrograde transport of mannose 6-phosphate receptors (MPRs) from endosomes to the TGN [PMID:9446797, PMID:18195106]. It was originally cloned as a syntaxin family member and localized to the TGN, where it colocalizes with the Golgi SNARE GS28 and is dispersed by brefeldin A but not wortmannin [PMID:9446797]. STX10 assembles into a quaternary SNARE complex with STX16, Vti1a, and VAMP3, and its depletion causes MPR missorting and hypersecretion of hexosaminidase, defining a route distinct from the STX6-dependent pathway used by TGN46 and cholera toxin [PMID:18195106]. This pathway is supported by the tether GCC185, which binds directly to STX16 in a manner competed by Rab6, consistent with GCC185 aiding delivery of Rab9-bearing vesicles to the TGN [PMID:18195106]. Notably, mouse and rat cells lack STX10 and use a different t-SNARE for this process [PMID:18195106]. Beyond this retrograde trafficking role, no further mechanistic detail has been characterized in the available corpus.","teleology":[{"year":1998,"claim":"Establishing where a newly identified syntaxin acts was the first step; cloning STX10 and localizing it to the TGN placed it within the secretory/endosomal membrane system.","evidence":"Indirect immunofluorescence and colocalization with Golgi marker GS28, with brefeldin A and wortmannin perturbation","pmids":["9446797"],"confidence":"Medium","gaps":["No SNARE partners or transport step identified","No functional assay linking localization to a trafficking pathway"]},{"year":2008,"claim":"Defined the molecular machinery and cargo specificity of STX10, showing it forms a distinct SNARE complex governing MPR retrograde transport rather than generic TGN traffic.","evidence":"siRNA depletion, reciprocal co-IP, hexosaminidase secretion and MPR trafficking assays, and direct GCC185-STX16 binding with Rab6 competition across multiple cell lines","pmids":["18195106"],"confidence":"High","gaps":["Structural basis of the STX10/STX16/Vti1a/VAMP3 complex not resolved","Identity of the t-SNARE used by mouse/rat cells lacking STX10 unknown","Mechanism by which GCC185-Rab6 regulation couples to vesicle delivery not fully defined"]},{"year":2021,"claim":"Probed STX10's wider interactome and infection-context behavior, identifying a candidate interaction with VAPB while exposing limitations of tagged constructs.","evidence":"BioID proximity labeling and fluorescence microscopy of BirA*-STX10 fusions during Chlamydia trachomatis and Coxiella burnetii infection","pmids":["34323972"],"confidence":"Low","gaps":["STX10-VAPB interaction not confirmed by an orthogonal method","BirA* tag altered STX10 localization, making the construct unreliable for infection trafficking studies","Functional consequence of any STX10-VAPB interaction unknown"]},{"year":null,"claim":"How STX10-dependent retrograde transport is regulated structurally and integrated with other interactors remains open.","evidence":"","pmids":[],"confidence":"Low","gaps":["No structural model of the STX10 SNARE complex","Physiological significance of the STX10-VAPB proximity interaction unestablished"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[1]}],"localization":[{"term_id":"GO:0005794","term_label":"Golgi apparatus","supporting_discovery_ids":[0,1]}],"pathway":[{"term_id":"R-HSA-5653656","term_label":"Vesicle-mediated transport","supporting_discovery_ids":[1]}],"complexes":["STX10/STX16/Vti1a/VAMP3 SNARE complex"],"partners":["STX16","VTI1A","VAMP3","GCC185","VAPB"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O60499","full_name":"Syntaxin-10","aliases":[],"length_aa":249,"mass_kda":28.1,"function":"SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network","subcellular_location":"Golgi apparatus membrane","url":"https://www.uniprot.org/uniprotkb/O60499/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/STX10","classification":"Not Classified","n_dependent_lines":38,"n_total_lines":1208,"dependency_fraction":0.03145695364238411},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000104915","cell_line_id":"CID000760","localizations":[{"compartment":"vesicles","grade":3},{"compartment":"er","grade":1},{"compartment":"membrane","grade":1}],"interactors":[{"gene":"STX16","stoichiometry":10.0},{"gene":"VTI1A","stoichiometry":10.0},{"gene":"STX16;STX16-NPEPL1","stoichiometry":4.0},{"gene":"VPS45","stoichiometry":4.0},{"gene":"CLTA","stoichiometry":0.2},{"gene":"VAMP4","stoichiometry":0.2},{"gene":"NSF","stoichiometry":0.2},{"gene":"SCFD1","stoichiometry":0.2},{"gene":"NAPA","stoichiometry":0.2},{"gene":"VAMP3;VAMP2","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/target/CID000760","total_profiled":1310},"omim":[{"mim_id":"615850","title":"VPS53 SUBUNIT OF GARP COMPLEX; VPS53","url":"https://www.omim.org/entry/615850"},{"mim_id":"614633","title":"VPS54 SUBUNIT OF GARP COMPLEX; VPS54","url":"https://www.omim.org/entry/614633"},{"mim_id":"603765","title":"SYNTAXIN 10; STX10","url":"https://www.omim.org/entry/603765"},{"mim_id":"603443","title":"VPS52 SUBUNIT OF GARP COMPLEX; VPS52","url":"https://www.omim.org/entry/603443"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Golgi apparatus","reliability":"Supported"},{"location":"Vesicles","reliability":"Supported"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/STX10"},"hgnc":{"alias_symbol":["hsyn10","SYN10"],"prev_symbol":[]},"alphafold":{"accession":"O60499","domains":[{"cath_id":"1.20.58.90","chopping":"1-122","consensus_level":"medium","plddt":87.7253,"start":1,"end":122},{"cath_id":"1.20.5","chopping":"215-247","consensus_level":"high","plddt":86.27,"start":215,"end":247}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O60499","model_url":"https://alphafold.ebi.ac.uk/files/AF-O60499-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O60499-F1-predicted_aligned_error_v6.png","plddt_mean":80.44},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=STX10","jax_strain_url":"https://www.jax.org/strain/search?query=STX10"},"sequence":{"accession":"O60499","fasta_url":"https://rest.uniprot.org/uniprotkb/O60499.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O60499/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O60499"}},"corpus_meta":[{"pmid":"31420334","id":"PMC_31420334","title":"Genomic and transcriptomic association studies identify 16 novel susceptibility loci for venous thromboembolism.","date":"2019","source":"Blood","url":"https://pubmed.ncbi.nlm.nih.gov/31420334","citation_count":185,"is_preprint":false},{"pmid":"18195106","id":"PMC_18195106","title":"A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells.","date":"2008","source":"The Journal of cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/18195106","citation_count":144,"is_preprint":false},{"pmid":"15288384","id":"PMC_15288384","title":"Narcotic antagonists in drug dependence: pilot study showing enhancement of compliance with SYN-10, amino-acid precursors and enkephalinase inhibition therapy.","date":"2004","source":"Medical hypotheses","url":"https://pubmed.ncbi.nlm.nih.gov/15288384","citation_count":47,"is_preprint":false},{"pmid":"21718468","id":"PMC_21718468","title":"Genome-wide expression quantitative trait loci (eQTL) analysis in maize.","date":"2011","source":"BMC genomics","url":"https://pubmed.ncbi.nlm.nih.gov/21718468","citation_count":47,"is_preprint":false},{"pmid":"32594266","id":"PMC_32594266","title":"A combination of linkage mapping and GWAS brings new elements on the genetic basis of yield-related traits in maize across multiple environments.","date":"2020","source":"TAG. 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This STX10-dependent route is distinct from the STX6-dependent route used by TGN46 and cholera toxin. Mouse and rat cells lack STX10 and must use a different t-SNARE for this process. Additionally, the tether GCC185 binds directly to STX16 and this interaction is competed by Rab6, supporting a model in which GCC185 helps Rab9-bearing vesicles deliver cargo to the trans-Golgi.\",\n      \"method\": \"siRNA depletion, co-immunoprecipitation, hexosaminidase secretion assay, MPR trafficking assay, direct binding assay (GCC185–STX16), Rab6 competition assay\",\n      \"journal\": \"The Journal of cell biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP, functional rescue, multiple orthogonal assays (secretion, trafficking, direct binding), replicated across multiple cell lines including mouse/rat lacking STX10\",\n      \"pmids\": [\"18195106\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Using BioID proximity labeling, a novel protein-protein interaction between STX10 and VAPB was identified. However, addition of the BirA* tag altered STX10 localization during Chlamydia trachomatis and Coxiella burnetii infection, indicating the fusion construct is not reliable for studying STX10 trafficking dynamics during intracellular pathogen infection.\",\n      \"method\": \"BioID proximity labeling, fluorescence microscopy of BirA*-Stx10 fusion constructs during infection\",\n      \"journal\": \"Pathogens and disease\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single proximity-labeling experiment, single lab, no validation of the STX10–VAPB interaction by orthogonal method\",\n      \"pmids\": [\"34323972\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"STX10 is a trans-Golgi network-localized t-SNARE that assembles into a quaternary SNARE complex with STX16, Vti1a, and VAMP3 to mediate the specific retrograde transport of mannose 6-phosphate receptors from late endosomes to the trans-Golgi network, a route distinct from the STX6-dependent pathway used by TGN46; the tether GCC185 facilitates this process by binding STX16 in a Rab6-regulated manner, and STX10 has also been found to interact with VAPB by proximity labeling.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"STX10 is a trans-Golgi network (TGN)-localized t-SNARE that mediates the specific retrograde transport of mannose 6-phosphate receptors (MPRs) from endosomes to the TGN [#0, #1]. It was originally cloned as a syntaxin family member and localized to the TGN, where it colocalizes with the Golgi SNARE GS28 and is dispersed by brefeldin A but not wortmannin [#0]. STX10 assembles into a quaternary SNARE complex with STX16, Vti1a, and VAMP3, and its depletion causes MPR missorting and hypersecretion of hexosaminidase, defining a route distinct from the STX6-dependent pathway used by TGN46 and cholera toxin [#1]. This pathway is supported by the tether GCC185, which binds directly to STX16 in a manner competed by Rab6, consistent with GCC185 aiding delivery of Rab9-bearing vesicles to the TGN [#1]. Notably, mouse and rat cells lack STX10 and use a different t-SNARE for this process [#1]. Beyond this retrograde trafficking role, no further mechanistic detail has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 1998,\n      \"claim\": \"Establishing where a newly identified syntaxin acts was the first step; cloning STX10 and localizing it to the TGN placed it within the secretory/endosomal membrane system.\",\n      \"evidence\": \"Indirect immunofluorescence and colocalization with Golgi marker GS28, with brefeldin A and wortmannin perturbation\",\n      \"pmids\": [\"9446797\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No SNARE partners or transport step identified\",\n        \"No functional assay linking localization to a trafficking pathway\"\n      ]\n    },\n    {\n      \"year\": 2008,\n      \"claim\": \"Defined the molecular machinery and cargo specificity of STX10, showing it forms a distinct SNARE complex governing MPR retrograde transport rather than generic TGN traffic.\",\n      \"evidence\": \"siRNA depletion, reciprocal co-IP, hexosaminidase secretion and MPR trafficking assays, and direct GCC185-STX16 binding with Rab6 competition across multiple cell lines\",\n      \"pmids\": [\"18195106\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural basis of the STX10/STX16/Vti1a/VAMP3 complex not resolved\",\n        \"Identity of the t-SNARE used by mouse/rat cells lacking STX10 unknown\",\n        \"Mechanism by which GCC185-Rab6 regulation couples to vesicle delivery not fully defined\"\n      ]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Probed STX10's wider interactome and infection-context behavior, identifying a candidate interaction with VAPB while exposing limitations of tagged constructs.\",\n      \"evidence\": \"BioID proximity labeling and fluorescence microscopy of BirA*-STX10 fusions during Chlamydia trachomatis and Coxiella burnetii infection\",\n      \"pmids\": [\"34323972\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"STX10-VAPB interaction not confirmed by an orthogonal method\",\n        \"BirA* tag altered STX10 localization, making the construct unreliable for infection trafficking studies\",\n        \"Functional consequence of any STX10-VAPB interaction unknown\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How STX10-dependent retrograde transport is regulated structurally and integrated with other interactors remains open.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No structural model of the STX10 SNARE complex\",\n        \"Physiological significance of the STX10-VAPB proximity interaction unestablished\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005794\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-5653656\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [\n      \"STX10/STX16/Vti1a/VAMP3 SNARE complex\"\n    ],\n    \"partners\": [\n      \"STX16\",\n      \"Vti1a\",\n      \"VAMP3\",\n      \"GCC185\",\n      \"VAPB\"\n    ],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":5,"faith_total":5,"faith_pct":100.0}}