{"gene":"TNPO1","run_date":"2026-04-28T21:42:59","timeline":{"discoveries":[{"year":1996,"finding":"Transportin (karyopherin-β2/TNPO1) was identified as a novel nuclear import receptor that binds the 38 amino acid M9 signal of hnRNP A1 and mediates its nuclear import through a pathway independent of the classical importin-α/β NLS pathway. Transportin is a ~90 kDa protein distantly related to importin-β.","method":"Co-immunoprecipitation of transportin with M9-containing proteins; in vitro nuclear import assays; mutational analysis of M9 signal distinguishing transport-competent from transport-defective variants","journal":"Cell","confidence":"High","confidence_rationale":"Tier 1-2 — original discovery using reconstituted import assays, binding specificity validated by transport-defective M9 mutants, foundational paper with >500 citations","pmids":["8808633"],"is_preprint":false},{"year":1995,"finding":"The M9 domain of hnRNP A1 functions as both a nuclear localization signal and a nuclear export signal, mediating bidirectional transport. Placing M9 on a nuclear-restricted protein (nucleoplasmin core domain) was sufficient to export it to the cytoplasm in a temperature-dependent manner, establishing M9 as a signal for a distinct export pathway.","method":"Fusion protein nuclear export assays; microinjection of M9-tagged nucleoplasmin core domain into Xenopus oocyte nuclei; temperature-sensitivity experiments","journal":"Cell","confidence":"High","confidence_rationale":"Tier 1-2 — direct functional reconstitution with heterologous fusion proteins; foundational paper with >480 citations","pmids":["8521471"],"is_preprint":false},{"year":1999,"finding":"The crystal structure of karyopherin-β2 (transportin/TNPO1) in complex with RanGppNHp was solved at 3.0 Å resolution. Karyopherin-β2 contains 18 HEAT repeats arranged into two orthogonal arches: Ran binds the N-terminal arch and the cargo/substrate-binding activity maps to the C-terminal arch. A large loop in HEAT repeat 7 spans both arches and is implicated in GTPase-mediated substrate dissociation in the nucleus.","method":"X-ray crystallography at 3.0 Å resolution; structure-based mapping of Ran and substrate binding sites","journal":"Nature","confidence":"High","confidence_rationale":"Tier 1 — high-resolution crystal structure with functional validation of binding domains; >300 citations","pmids":["10353245"],"is_preprint":false},{"year":1998,"finding":"Transportin (TNPO1) directly binds and imports ribosomal proteins (e.g., rpL23a, rpS7, rpL5) into the nucleus in mammalian cells, acting as one of at least four importin-β-like transport receptors for ribosomal proteins. The classical importin-α/β heterodimer pathway plays only a minor role in ribosomal protein import. A very basic region in rpL23a serves as the binding site recognized by transportin.","method":"In vitro nuclear import assays in digitonin-permeabilized mammalian cells; direct binding assays between recombinant transportin and ribosomal proteins; identification of minimal import signals by deletion analysis","journal":"The EMBO journal","confidence":"High","confidence_rationale":"Tier 1-2 — reconstituted import assays with multiple substrates and multiple receptors, domain mapping; >430 citations","pmids":["9687515"],"is_preprint":false},{"year":2010,"finding":"TNPO1 (transportin) mediates nuclear import of the ALS-associated RNA-binding protein FUS via a non-classical PY-NLS located in the C-terminus of FUS. Familial ALS mutations predominantly cluster within this PY-NLS and impair nuclear import in a manner correlating with age of disease onset. Disruption of the transportin-mediated import pathway leads to cytoplasmic redistribution of FUS and its recruitment into stress granules.","method":"Nuclear import assays; co-immunoprecipitation of FUS with transportin; mapping of NLS by deletion/mutation analysis; live-cell imaging; immunofluorescence in patient tissue; siRNA knockdown of transportin","journal":"The EMBO journal","confidence":"High","confidence_rationale":"Tier 1-2 — multiple orthogonal methods (binding assays, import reconstitution, mutagenesis, patient tissue validation); >680 citations","pmids":["20606625"],"is_preprint":false},{"year":2014,"finding":"In Drosophila, Transportin (Trn, ortholog of mammalian TNPO1/Kapβ2) mediates nuclear import of the transcription factor Ci (Gli) via a PY-NLS located in the N-terminal conserved domain of Ci. Sufu (Suppressor of fused) opposes Trn-mediated Ci nuclear import by masking the PY-NLS. Mammalian Gli proteins also contain a functional PY-NLS, and mammalian Sufu uses a similar mechanism to regulate Gli nuclear translocation.","method":"Identification and mutational analysis of PY-NLS in Ci/Gli; epistasis experiments in Drosophila hedgehog signaling; co-immunoprecipitation of Trn with Ci; rescue experiments; Sufu masking assays","journal":"Journal of cell science","confidence":"High","confidence_rationale":"Tier 2 — genetic epistasis, Co-IP, mutagenesis in Drosophila ortholog with mammalian validation; multiple orthogonal methods","pmids":["24413177"],"is_preprint":false},{"year":2017,"finding":"TNPO1 is required for nuclear import of LINE-1 (L1) ribonucleoprotein complexes and promotes L1 retrotransposition. miR-128 targets the 3' UTR of TNPO1 mRNA to repress its expression, thereby restricting L1 activity in somatic cells. Depletion of TNPO1 reduced L1 retrotransposition and nuclear import of L1-encoded ORF1p (used as a proxy for L1-RNP), while TNPO1 overexpression partially reversed miR-128-mediated repression of L1 retrotransposition.","method":"miR-128 mimic/inhibitor transfection; TNPO1 siRNA knockdown and overexpression; L1 retrotransposition reporter assays; nuclear import assays using L1 ORF1p as proxy; 3' UTR luciferase reporter assay validating miR-128 targeting","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2-3 — functional knockdown/overexpression with specific phenotypic readout (retrotransposition and nuclear import); single lab, multiple methods","pmids":["28974576"],"is_preprint":false}],"current_model":"TNPO1 (transportin/karyopherin-β2) is a nuclear import receptor containing 18 HEAT repeats that recognizes non-classical PY-NLS signals (as in hnRNP A1 M9, FUS) and mediates cargo nuclear import in a RanGTP-dependent manner; structurally, RanGTP binds its N-terminal arch to displace cargo from the C-terminal arch, enabling substrate release in the nucleus; its substrates include shuttling hnRNPs, ribosomal proteins, Gli/Ci transcription factors, and LINE-1 RNP complexes, and disease-causing mutations in PY-NLS-containing proteins (e.g., ALS-associated FUS mutations) impair TNPO1-mediated import leading to cytoplasmic mislocalization and stress granule recruitment."},"narrative":{"teleology":[{"year":1995,"claim":"Demonstration that the M9 domain of hnRNP A1 functions as both a nuclear import and export signal established the existence of a bidirectional transport pathway distinct from the classical NLS route, raising the question of which receptor mediates this pathway.","evidence":"Microinjection of M9-tagged fusion proteins into Xenopus oocyte nuclei with temperature-sensitivity controls","pmids":["8521471"],"confidence":"High","gaps":["Identity of the receptor recognizing M9 was unknown","Mechanism of bidirectional signaling by a single peptide was unexplained"]},{"year":1996,"claim":"Identification of transportin (TNPO1) as the ~90 kDa import receptor that directly binds the M9 signal answered the receptor-identity question and defined a non-classical nuclear import pathway parallel to importin-α/β.","evidence":"Co-immunoprecipitation of transportin with M9-containing proteins and reconstituted in vitro nuclear import assays in permeabilized cells","pmids":["8808633"],"confidence":"High","gaps":["Structural basis of cargo recognition was unknown","Range of substrates beyond hnRNP A1 was uncharacterized","Mechanism of cargo release in the nucleus was unclear"]},{"year":1998,"claim":"Showing that transportin directly imports ribosomal proteins (rpL23a, rpS7, rpL5) via basic-region signals expanded the substrate repertoire well beyond shuttling hnRNPs and indicated that TNPO1 recognizes diverse signal types.","evidence":"Reconstituted nuclear import assays in digitonin-permeabilized mammalian cells with deletion mapping of import signals","pmids":["9687515"],"confidence":"High","gaps":["Consensus features distinguishing transportin-recognized signals from classical NLSs were not yet defined","Relative contribution of transportin versus other importin-β family members for ribosomal protein import was uncertain"]},{"year":1999,"claim":"The 3.0 Å crystal structure of TNPO1 bound to RanGppNHp revealed the 18-HEAT-repeat, two-arch architecture and showed how RanGTP binding to the N-terminal arch allosterically promotes cargo release from the C-terminal arch, providing the first structural explanation for the import cycle.","evidence":"X-ray crystallography of karyopherin-β2–RanGppNHp complex with structure-based mapping of functional domains","pmids":["10353245"],"confidence":"High","gaps":["No co-crystal with a PY-NLS cargo was available","Role of the HEAT-repeat 7 loop in substrate dissociation was inferred but not directly tested by mutagenesis in this study"]},{"year":2010,"claim":"Mapping the PY-NLS of FUS as the transportin-binding element and showing that ALS-causing mutations within it impair nuclear import in proportion to clinical severity directly linked TNPO1-dependent transport to neurodegenerative disease pathogenesis.","evidence":"Nuclear import assays, co-immunoprecipitation, mutagenesis, live-cell imaging, siRNA knockdown of transportin, and immunofluorescence in patient tissue","pmids":["20606625"],"confidence":"High","gaps":["Whether restoring TNPO1-mediated import could rescue disease phenotypes in vivo was untested","Contribution of stress-granule sequestration versus loss of nuclear function to neurodegeneration was unresolved"]},{"year":2014,"claim":"Identification of a conserved PY-NLS in Ci/Gli transcription factors and demonstration that Sufu masks this signal to block TNPO1-mediated nuclear entry connected transportin to Hedgehog signaling and illustrated a regulatory strategy in which co-factors modulate import by NLS masking.","evidence":"PY-NLS mutagenesis, co-immunoprecipitation of Trn with Ci, genetic epistasis in Drosophila Hedgehog pathway, and mammalian Gli validation","pmids":["24413177"],"confidence":"High","gaps":["Structural basis of Sufu masking of the PY-NLS was not determined","Whether other signaling pathways regulate cargo access to TNPO1 by analogous masking was unknown"]},{"year":2017,"claim":"Demonstrating that TNPO1 mediates nuclear import of LINE-1 ribonucleoprotein complexes and that miR-128 represses TNPO1 expression to restrict retrotransposition revealed a role for transportin in transposable element biology and a post-transcriptional regulatory layer controlling its abundance.","evidence":"TNPO1 knockdown/overexpression, L1 retrotransposition reporter assays, ORF1p nuclear import assays, and 3′ UTR luciferase reporters for miR-128 targeting","pmids":["28974576"],"confidence":"Medium","gaps":["Direct physical interaction between TNPO1 and L1-RNP was not demonstrated with purified components","Whether TNPO1 recognizes a PY-NLS-like motif in L1 ORF1p or ORF2p was not mapped","Findings from a single laboratory"]},{"year":null,"claim":"A comprehensive structural picture of TNPO1 bound to its diverse PY-NLS cargoes (FUS, Gli, ribosomal proteins, L1-RNP) is still incomplete, and whether therapeutic modulation of TNPO1-mediated import can ameliorate ALS or other proteinopathies remains an open question.","evidence":"","pmids":[],"confidence":"Low","gaps":["No co-crystal structures with FUS, Gli, or ribosomal protein PY-NLS cargoes described in this timeline","In vivo therapeutic relevance of restoring TNPO1-mediated FUS import in ALS models is untested","Regulatory mechanisms controlling TNPO1 expression beyond miR-128 are uncharacterized"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0005215","term_label":"transporter activity","supporting_discovery_ids":[0,3,4,5,6]},{"term_id":"GO:0038024","term_label":"cargo receptor activity","supporting_discovery_ids":[0,3,4,5]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[0,2,3,4,5]},{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[0,4]}],"pathway":[{"term_id":"R-HSA-9609507","term_label":"Protein localization","supporting_discovery_ids":[0,2,3,4,5,6]}],"complexes":[],"partners":["HNRNPA1","FUS","RAN","RPL23A","RPS7","RPL5","GLI2","SUFU"],"other_free_text":[]},"mechanistic_narrative":"TNPO1 (transportin-1/karyopherin-β2) is a RanGTP-regulated nuclear import receptor that recognizes non-classical proline-tyrosine nuclear localization signals (PY-NLS) and mediates translocation of diverse cargoes—including shuttling hnRNPs, ribosomal proteins, Gli/Ci transcription factors, and LINE-1 ribonucleoprotein complexes—through the nuclear pore complex [PMID:8808633, PMID:9687515, PMID:24413177, PMID:28974576]. Its 18 HEAT-repeat structure forms two orthogonal arches: RanGTP binds the N-terminal arch and allosterically triggers cargo release from the C-terminal arch, with a critical loop in HEAT repeat 7 coupling these events [PMID:10353245]. The M9 signal of hnRNP A1, the founding PY-NLS, functions as both a nuclear import and nuclear export signal, establishing a bidirectional transport pathway [PMID:8521471, PMID:8808633]. Familial ALS mutations in the PY-NLS of FUS impair TNPO1-mediated import in proportion to disease severity, leading to cytoplasmic FUS accumulation and stress-granule recruitment [PMID:20606625]."},"prefetch_data":{"uniprot":{"accession":"Q92973","full_name":"Transportin-1","aliases":["Importin beta-2","Karyopherin beta-2","M9 region interaction protein","MIP"],"length_aa":898,"mass_kda":102.4,"function":"Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates (PubMed:24753571). May mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5 (PubMed:11682607). In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones (By similarity). In vitro, mediates nuclear import of SRP19 (PubMed:11682607). Mediates nuclear import of ADAR/ADAR1 isoform 1 and isoform 5 in a RanGTP-dependent manner (PubMed:19124606, PubMed:24753571). Main mediator of PR-DUB complex component BAP1 nuclear import; acts redundantly with the karyopherins KPNA1 and KPNA2 (PubMed:35446349) (Microbial infection) In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev","subcellular_location":"Cytoplasm; Nucleus","url":"https://www.uniprot.org/uniprotkb/Q92973/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/TNPO1","classification":"Not Classified","n_dependent_lines":466,"n_total_lines":1208,"dependency_fraction":0.38576158940397354},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000083312","cell_line_id":"CID001576","localizations":[{"compartment":"cytoplasmic","grade":3},{"compartment":"nuclear_membrane","grade":3},{"compartment":"nucleoplasm","grade":3},{"compartment":"big_aggregates","grade":2}],"interactors":[{"gene":"NUP153","stoichiometry":10.0},{"gene":"TMA16","stoichiometry":10.0},{"gene":"ALYREF","stoichiometry":10.0},{"gene":"FUS","stoichiometry":4.0},{"gene":"HNRNPD","stoichiometry":4.0},{"gene":"CAPZB","stoichiometry":0.2},{"gene":"EWSR1","stoichiometry":0.2},{"gene":"HNRNPA0","stoichiometry":0.2},{"gene":"HNRNPA2B1","stoichiometry":0.2},{"gene":"HNRNPH1","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/target/CID001576","total_profiled":1310},"omim":[{"mim_id":"620460","title":"OCULOPHARYNGEAL MUSCULAR DYSTROPHY 2; OPMD2","url":"https://www.omim.org/entry/620460"},{"mim_id":"620067","title":"CARDIAC VALVULAR DYSPLASIA 2; CVDP2","url":"https://www.omim.org/entry/620067"},{"mim_id":"616642","title":"CHROMOSOME 6 OPEN READING FRAME 89; C6ORF89","url":"https://www.omim.org/entry/616642"},{"mim_id":"615587","title":"NUCLEOPORIN, 188-KD; NUP188","url":"https://www.omim.org/entry/615587"},{"mim_id":"614951","title":"HEAT REPEAT-CONTAINING PROTEIN 3; HEATR3","url":"https://www.omim.org/entry/614951"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Nucleoplasm","reliability":"Supported"},{"location":"Nucleoli","reliability":"Additional"},{"location":"Cytosol","reliability":"Additional"},{"location":"Cytoplasmic bodies","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/TNPO1"},"hgnc":{"alias_symbol":["MIP","TRN","IPO2","MIP1"],"prev_symbol":["KPNB2"]},"alphafold":{"accession":"Q92973","domains":[{"cath_id":"1.25.10","chopping":"720-898","consensus_level":"medium","plddt":94.8025,"start":720,"end":898}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q92973","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q92973-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q92973-F1-predicted_aligned_error_v6.png","plddt_mean":92.44},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=TNPO1","jax_strain_url":"https://www.jax.org/strain/search?query=TNPO1"},"sequence":{"accession":"Q92973","fasta_url":"https://rest.uniprot.org/uniprotkb/Q92973.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q92973/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q92973"}},"corpus_meta":[{"pmid":"8525373","id":"PMC_8525373","title":"Identification 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of Sciences of the United States of America","url":"https://pubmed.ncbi.nlm.nih.gov/9275210","citation_count":415,"is_preprint":false,"source_track":"gene2pubmed"},{"pmid":"26344197","id":"PMC_26344197","title":"Panorama of ancient metazoan macromolecular complexes.","date":"2015","source":"Nature","url":"https://pubmed.ncbi.nlm.nih.gov/26344197","citation_count":407,"is_preprint":false,"source_track":"gene2pubmed"},{"pmid":"17643375","id":"PMC_17643375","title":"Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme.","date":"2007","source":"Molecular cell","url":"https://pubmed.ncbi.nlm.nih.gov/17643375","citation_count":367,"is_preprint":false,"source_track":"gene2pubmed"},{"pmid":"9891055","id":"PMC_9891055","title":"The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals.","date":"1999","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/9891055","citation_count":357,"is_preprint":false,"source_track":"gene2pubmed"},{"pmid":"34079125","id":"PMC_34079125","title":"A proximity-dependent biotinylation map of a human cell.","date":"2021","source":"Nature","url":"https://pubmed.ncbi.nlm.nih.gov/34079125","citation_count":339,"is_preprint":false,"source_track":"gene2pubmed"},{"pmid":"22810586","id":"PMC_22810586","title":"Interpreting cancer genomes using systematic host network perturbations by tumour virus proteins.","date":"2012","source":"Nature","url":"https://pubmed.ncbi.nlm.nih.gov/22810586","citation_count":319,"is_preprint":false,"source_track":"gene2pubmed"},{"pmid":"27342126","id":"PMC_27342126","title":"Identification of Zika Virus and Dengue Virus Dependency Factors using Functional Genomics.","date":"2016","source":"Cell 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standard","round2_stage1":{"model":"claude-sonnet-4-6","input_tokens":60251,"output_tokens":2574,"usd":0.109682},"round2_rules_fired":"R2,R3","round2_stage2":{"model":"claude-opus-4-6","input_tokens":5684,"output_tokens":2269,"usd":0.127718}},"stage1_raw":"Looking through the abstracts, I need to identify papers about TNPO1 (Transportin 1, also known as Kapβ2 or TRN). Let me carefully distinguish between TNPO1 and its paralog TNPO3 (TRN-SR2), and filter out unrelated genes sharing \"MIP\" or other symbols.\n\nRelevant papers for TNPO1:\n- PMID 28974576: miR-128 targets TNPO1 to control LINE-1 retrotransposition\n- PMID 24413177: Transportin (Drosophila homolog of Kapβ2/TNPO1) mediates Ci/Gli nuclear import via PY-NLS; Sufu opposes this\n\nPapers about TNPO3 (TRN-SR2, a different gene): PMIDs 19846519, 22872640, 25063804 — these are about TNPO3, not TNPO1.\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2017,\n      \"finding\": \"TNPO1 (Transportin 1) mediates nuclear import of the LINE-1 ribonucleoprotein complex (using L1-encoded ORF1p as a proxy); depletion of TNPO1 reduces L1 retrotransposition, and TNPO1 overexpression partially reverses the repressive effect of miR-128 on L1 retrotransposition, demonstrating a direct role for TNPO1 in nuclear import of the L1 element.\",\n      \"method\": \"siRNA knockdown and overexpression of TNPO1 combined with L1 retrotransposition reporter assays and nuclear import assays; miR-128 targeting of TNPO1 3' UTR validated\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — clean KD/OE with defined cellular phenotype (L1 retrotransposition and nuclear import), single lab\",\n      \"pmids\": [\"28974576\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"Transportin (Drosophila homolog of mammalian Kapβ2/TNPO1) mediates PY-NLS-dependent nuclear import of the Hedgehog pathway transcription factor Ci/Gli; Suppressor of fused (Sufu) blocks this nuclear import by masking the PY-NLS of Ci, and mammalian Sufu uses a similar mechanism to regulate Gli nuclear translocation.\",\n      \"method\": \"Genetic epistasis in Drosophila, identification of novel PY-NLS in Ci/Gli N-terminal domain, in vivo localization studies, dominant-negative and rescue experiments; mammalian Gli PY-NLS validated in cell-based assays\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal methods (NLS mapping, epistasis, localization, functional rescue) in both Drosophila and mammalian systems\",\n      \"pmids\": [\"24413177\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"TNPO1 (Transportin 1/Kapβ2) functions as a nuclear import receptor that recognizes PY-NLS-containing cargoes—including Gli/Ci transcription factors (whose import is opposed by Sufu) and LINE-1 ribonucleoprotein complexes—and is itself regulated post-transcriptionally by miR-128, which reduces TNPO1 levels to restrict L1 retrotransposition.\"\n}\n```\n\n--- ROUND 2 (R2/R3, augmented corpus) ---\n\nI'll classify each paper and extract discoveries only from KEEP papers.\n\n**Classification summary:**\n- Papers [1]-[100] in the retrieved corpus: Nearly all are about MIP-1α/β chemokines (CCL3/CCL4), aquaporin MIP (AQP0), Legionella Mip, mitochondrial MIP, or other unrelated proteins. These are EXCLUDE (alias collisions).\n- Paper [91] (PMID:28974576): Describes TNPO1 (transportin 1) — KEEP\n- Additional papers [13] (PMID:20606625), [15] (PMID:8808633), [18] (PMID:8521471), [22] (PMID:9687515), [30] (PMID:10353245): Describe transportin/Kapβ2 (TNPO1/Karyopherin-β2) — KEEP\n- Paper [72] (PMID:24413177): Describes Transportin (Trn/Kapβ2) mediating Ci/Gli nuclear import — KEEP (ortholog study in Drosophila, consistent with mammalian TNPO1 function)\n- Papers [20] (PMID:19846519), [57] (PMID:22872640), [97] (PMID:25063804): About TNPO3 (transportin-3/TRN-SR2), not TNPO1 — EXCLUDE\n- Additional papers [1]-[12], [14], [16]-[17], [19]-[21], [23]-[29]: Large-scale proteomics/interactome datasets or HIV nuclear import papers not specifically about TNPO1 mechanism — most EXCLUDE except where TNPO1 mechanism is directly described.\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1996,\n      \"finding\": \"Transportin (karyopherin-β2/TNPO1) was identified as a novel nuclear import receptor that binds the 38 amino acid M9 signal of hnRNP A1 and mediates its nuclear import through a pathway independent of the classical importin-α/β NLS pathway. Transportin is a ~90 kDa protein distantly related to importin-β.\",\n      \"method\": \"Co-immunoprecipitation of transportin with M9-containing proteins; in vitro nuclear import assays; mutational analysis of M9 signal distinguishing transport-competent from transport-defective variants\",\n      \"journal\": \"Cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 — original discovery using reconstituted import assays, binding specificity validated by transport-defective M9 mutants, foundational paper with >500 citations\",\n      \"pmids\": [\"8808633\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1995,\n      \"finding\": \"The M9 domain of hnRNP A1 functions as both a nuclear localization signal and a nuclear export signal, mediating bidirectional transport. Placing M9 on a nuclear-restricted protein (nucleoplasmin core domain) was sufficient to export it to the cytoplasm in a temperature-dependent manner, establishing M9 as a signal for a distinct export pathway.\",\n      \"method\": \"Fusion protein nuclear export assays; microinjection of M9-tagged nucleoplasmin core domain into Xenopus oocyte nuclei; temperature-sensitivity experiments\",\n      \"journal\": \"Cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 — direct functional reconstitution with heterologous fusion proteins; foundational paper with >480 citations\",\n      \"pmids\": [\"8521471\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1999,\n      \"finding\": \"The crystal structure of karyopherin-β2 (transportin/TNPO1) in complex with RanGppNHp was solved at 3.0 Å resolution. Karyopherin-β2 contains 18 HEAT repeats arranged into two orthogonal arches: Ran binds the N-terminal arch and the cargo/substrate-binding activity maps to the C-terminal arch. A large loop in HEAT repeat 7 spans both arches and is implicated in GTPase-mediated substrate dissociation in the nucleus.\",\n      \"method\": \"X-ray crystallography at 3.0 Å resolution; structure-based mapping of Ran and substrate binding sites\",\n      \"journal\": \"Nature\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 — high-resolution crystal structure with functional validation of binding domains; >300 citations\",\n      \"pmids\": [\"10353245\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1998,\n      \"finding\": \"Transportin (TNPO1) directly binds and imports ribosomal proteins (e.g., rpL23a, rpS7, rpL5) into the nucleus in mammalian cells, acting as one of at least four importin-β-like transport receptors for ribosomal proteins. The classical importin-α/β heterodimer pathway plays only a minor role in ribosomal protein import. A very basic region in rpL23a serves as the binding site recognized by transportin.\",\n      \"method\": \"In vitro nuclear import assays in digitonin-permeabilized mammalian cells; direct binding assays between recombinant transportin and ribosomal proteins; identification of minimal import signals by deletion analysis\",\n      \"journal\": \"The EMBO journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 — reconstituted import assays with multiple substrates and multiple receptors, domain mapping; >430 citations\",\n      \"pmids\": [\"9687515\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"TNPO1 (transportin) mediates nuclear import of the ALS-associated RNA-binding protein FUS via a non-classical PY-NLS located in the C-terminus of FUS. Familial ALS mutations predominantly cluster within this PY-NLS and impair nuclear import in a manner correlating with age of disease onset. Disruption of the transportin-mediated import pathway leads to cytoplasmic redistribution of FUS and its recruitment into stress granules.\",\n      \"method\": \"Nuclear import assays; co-immunoprecipitation of FUS with transportin; mapping of NLS by deletion/mutation analysis; live-cell imaging; immunofluorescence in patient tissue; siRNA knockdown of transportin\",\n      \"journal\": \"The EMBO journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 — multiple orthogonal methods (binding assays, import reconstitution, mutagenesis, patient tissue validation); >680 citations\",\n      \"pmids\": [\"20606625\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"In Drosophila, Transportin (Trn, ortholog of mammalian TNPO1/Kapβ2) mediates nuclear import of the transcription factor Ci (Gli) via a PY-NLS located in the N-terminal conserved domain of Ci. Sufu (Suppressor of fused) opposes Trn-mediated Ci nuclear import by masking the PY-NLS. Mammalian Gli proteins also contain a functional PY-NLS, and mammalian Sufu uses a similar mechanism to regulate Gli nuclear translocation.\",\n      \"method\": \"Identification and mutational analysis of PY-NLS in Ci/Gli; epistasis experiments in Drosophila hedgehog signaling; co-immunoprecipitation of Trn with Ci; rescue experiments; Sufu masking assays\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — genetic epistasis, Co-IP, mutagenesis in Drosophila ortholog with mammalian validation; multiple orthogonal methods\",\n      \"pmids\": [\"24413177\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"TNPO1 is required for nuclear import of LINE-1 (L1) ribonucleoprotein complexes and promotes L1 retrotransposition. miR-128 targets the 3' UTR of TNPO1 mRNA to repress its expression, thereby restricting L1 activity in somatic cells. Depletion of TNPO1 reduced L1 retrotransposition and nuclear import of L1-encoded ORF1p (used as a proxy for L1-RNP), while TNPO1 overexpression partially reversed miR-128-mediated repression of L1 retrotransposition.\",\n      \"method\": \"miR-128 mimic/inhibitor transfection; TNPO1 siRNA knockdown and overexpression; L1 retrotransposition reporter assays; nuclear import assays using L1 ORF1p as proxy; 3' UTR luciferase reporter assay validating miR-128 targeting\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 — functional knockdown/overexpression with specific phenotypic readout (retrotransposition and nuclear import); single lab, multiple methods\",\n      \"pmids\": [\"28974576\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"TNPO1 (transportin/karyopherin-β2) is a nuclear import receptor containing 18 HEAT repeats that recognizes non-classical PY-NLS signals (as in hnRNP A1 M9, FUS) and mediates cargo nuclear import in a RanGTP-dependent manner; structurally, RanGTP binds its N-terminal arch to displace cargo from the C-terminal arch, enabling substrate release in the nucleus; its substrates include shuttling hnRNPs, ribosomal proteins, Gli/Ci transcription factors, and LINE-1 RNP complexes, and disease-causing mutations in PY-NLS-containing proteins (e.g., ALS-associated FUS mutations) impair TNPO1-mediated import leading to cytoplasmic mislocalization and stress granule recruitment.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"TNPO1 (Transportin 1/Kapβ2) is a nuclear import receptor that recognizes PY-NLS motifs to transport cargo proteins into the nucleus. TNPO1 mediates PY-NLS-dependent nuclear import of the Hedgehog pathway transcription factors Ci/Gli, a process antagonized by Suppressor of Fused (Sufu), which masks the PY-NLS on Ci/Gli to prevent nuclear translocation [PMID:24413177]. TNPO1 also facilitates nuclear import of the LINE-1 ribonucleoprotein complex, and its depletion reduces L1 retrotransposition; miR-128 post-transcriptionally represses TNPO1 to restrict L1 activity [PMID:28974576].\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Establishing that TNPO1/Transportin recognizes a PY-NLS in Ci/Gli transcription factors resolved how Hedgehog pathway effectors enter the nucleus and revealed that Sufu antagonizes this import by masking the NLS, linking nuclear transport regulation directly to developmental signaling.\",\n      \"evidence\": \"Genetic epistasis, NLS mapping, localization assays, and rescue experiments in Drosophila with validation of mammalian Gli PY-NLS in cell-based assays\",\n      \"pmids\": [\"24413177\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural basis of Sufu masking of the PY-NLS has not been determined\",\n        \"Whether other Hedgehog pathway components modulate the TNPO1–Gli interaction is unknown\",\n        \"Relative contributions of TNPO1 versus other importins to Gli nuclear import in different tissue contexts remain uncharacterized\"\n      ]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Demonstrating that TNPO1 imports the LINE-1 ribonucleoprotein complex into the nucleus expanded its cargo repertoire beyond classical transcription factors and uncovered miR-128-mediated post-transcriptional regulation of TNPO1 as a host defense mechanism against retrotransposition.\",\n      \"evidence\": \"siRNA knockdown and overexpression of TNPO1 combined with L1 retrotransposition reporter assays; miR-128 targeting of TNPO1 3′ UTR validated\",\n      \"pmids\": [\"28974576\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct physical interaction between TNPO1 and L1 ORF1p/RNP has not been demonstrated by reciprocal co-immunoprecipitation or reconstitution\",\n        \"Whether TNPO1 recognizes a canonical PY-NLS or an alternative motif on the L1 RNP is unknown\",\n        \"Physiological relevance of miR-128-mediated TNPO1 regulation in specific tissues has not been established\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The full spectrum of TNPO1 cargoes in vivo, the structural determinants governing cargo selectivity versus other β-karyopherins, and the in vivo consequences of TNPO1 loss in mammalian development remain to be defined.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No mammalian genetic loss-of-function model has been reported\",\n        \"Comprehensive cargo profiling for TNPO1 has not been performed\",\n        \"No structural model of TNPO1 bound to the Ci/Gli PY-NLS exists\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005215\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0009607\", \"supporting_discovery_ids\": []},\n      {\"term_id\": \"R-HSA-9609507\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"GLI1\",\n      \"SUFU\",\n      \"ORF1P\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```\n\nWait, I need to fix the pathway entry — I included an invalid GO term. Let me correct:\n\n```json\n{\n  \"mechanistic_narrative\": \"TNPO1 (Transportin 1/Kapβ2) is a nuclear import receptor that recognizes PY-NLS motifs to transport cargo proteins into the nucleus. TNPO1 mediates PY-NLS-dependent nuclear import of the Hedgehog pathway transcription factors Ci/Gli, a process antagonized by Suppressor of Fused (Sufu), which masks the PY-NLS on Ci/Gli to prevent nuclear translocation [PMID:24413177]. TNPO1 also facilitates nuclear import of the LINE-1 ribonucleoprotein complex, and its depletion reduces L1 retrotransposition; miR-128 post-transcriptionally represses TNPO1 to restrict L1 activity [PMID:28974576].\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Establishing that TNPO1/Transportin recognizes a PY-NLS in Ci/Gli transcription factors resolved how Hedgehog pathway effectors enter the nucleus and revealed that Sufu antagonizes this import by masking the NLS, linking nuclear transport regulation directly to developmental signaling.\",\n      \"evidence\": \"Genetic epistasis, NLS mapping, localization assays, and rescue experiments in Drosophila with validation of mammalian Gli PY-NLS in cell-based assays\",\n      \"pmids\": [\"24413177\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural basis of Sufu masking of the PY-NLS has not been determined\",\n        \"Whether other Hedgehog pathway components modulate the TNPO1–Gli interaction is unknown\",\n        \"Relative contributions of TNPO1 versus other importins to Gli nuclear import in different tissue contexts remain uncharacterized\"\n      ]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Demonstrating that TNPO1 imports the LINE-1 ribonucleoprotein complex into the nucleus expanded its cargo repertoire beyond classical transcription factors and uncovered miR-128-mediated post-transcriptional regulation of TNPO1 as a host defense mechanism against retrotransposition.\",\n      \"evidence\": \"siRNA knockdown and overexpression of TNPO1 combined with L1 retrotransposition reporter assays; miR-128 targeting of TNPO1 3′ UTR validated\",\n      \"pmids\": [\"28974576\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct physical interaction between TNPO1 and L1 ORF1p/RNP has not been demonstrated by reciprocal co-immunoprecipitation or reconstitution\",\n        \"Whether TNPO1 recognizes a canonical PY-NLS or an alternative motif on the L1 RNP is unknown\",\n        \"Physiological relevance of miR-128-mediated TNPO1 regulation in specific tissues has not been established\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The full spectrum of TNPO1 cargoes in vivo, the structural determinants governing cargo selectivity versus other β-karyopherins, and the in vivo consequences of TNPO1 loss in mammalian development remain to be defined.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No mammalian genetic loss-of-function model has been reported\",\n        \"Comprehensive cargo profiling for TNPO1 has not been performed\",\n        \"No structural model of TNPO1 bound to the Ci/Gli PY-NLS exists\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005215\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-9609507\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"SUFU\",\n      \"ORF1P\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```\n\n--- ROUND 2 (R2/R3, augmented corpus) ---\n\n```json\n{\n  \"mechanistic_narrative\": \"TNPO1 (transportin-1/karyopherin-β2) is a RanGTP-regulated nuclear import receptor that recognizes non-classical proline-tyrosine nuclear localization signals (PY-NLS) and mediates translocation of diverse cargoes—including shuttling hnRNPs, ribosomal proteins, Gli/Ci transcription factors, and LINE-1 ribonucleoprotein complexes—through the nuclear pore complex [PMID:8808633, PMID:9687515, PMID:24413177, PMID:28974576]. Its 18 HEAT-repeat structure forms two orthogonal arches: RanGTP binds the N-terminal arch and allosterically triggers cargo release from the C-terminal arch, with a critical loop in HEAT repeat 7 coupling these events [PMID:10353245]. The M9 signal of hnRNP A1, the founding PY-NLS, functions as both a nuclear import and nuclear export signal, establishing a bidirectional transport pathway [PMID:8521471, PMID:8808633]. Familial ALS mutations in the PY-NLS of FUS impair TNPO1-mediated import in proportion to disease severity, leading to cytoplasmic FUS accumulation and stress-granule recruitment [PMID:20606625].\",\n  \"teleology\": [\n    {\n      \"year\": 1995,\n      \"claim\": \"Demonstration that the M9 domain of hnRNP A1 functions as both a nuclear import and export signal established the existence of a bidirectional transport pathway distinct from the classical NLS route, raising the question of which receptor mediates this pathway.\",\n      \"evidence\": \"Microinjection of M9-tagged fusion proteins into Xenopus oocyte nuclei with temperature-sensitivity controls\",\n      \"pmids\": [\"8521471\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Identity of the receptor recognizing M9 was unknown\", \"Mechanism of bidirectional signaling by a single peptide was unexplained\"]\n    },\n    {\n      \"year\": 1996,\n      \"claim\": \"Identification of transportin (TNPO1) as the ~90 kDa import receptor that directly binds the M9 signal answered the receptor-identity question and defined a non-classical nuclear import pathway parallel to importin-α/β.\",\n      \"evidence\": \"Co-immunoprecipitation of transportin with M9-containing proteins and reconstituted in vitro nuclear import assays in permeabilized cells\",\n      \"pmids\": [\"8808633\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of cargo recognition was unknown\", \"Range of substrates beyond hnRNP A1 was uncharacterized\", \"Mechanism of cargo release in the nucleus was unclear\"]\n    },\n    {\n      \"year\": 1998,\n      \"claim\": \"Showing that transportin directly imports ribosomal proteins (rpL23a, rpS7, rpL5) via basic-region signals expanded the substrate repertoire well beyond shuttling hnRNPs and indicated that TNPO1 recognizes diverse signal types.\",\n      \"evidence\": \"Reconstituted nuclear import assays in digitonin-permeabilized mammalian cells with deletion mapping of import signals\",\n      \"pmids\": [\"9687515\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Consensus features distinguishing transportin-recognized signals from classical NLSs were not yet defined\", \"Relative contribution of transportin versus other importin-β family members for ribosomal protein import was uncertain\"]\n    },\n    {\n      \"year\": 1999,\n      \"claim\": \"The 3.0 Å crystal structure of TNPO1 bound to RanGppNHp revealed the 18-HEAT-repeat, two-arch architecture and showed how RanGTP binding to the N-terminal arch allosterically promotes cargo release from the C-terminal arch, providing the first structural explanation for the import cycle.\",\n      \"evidence\": \"X-ray crystallography of karyopherin-β2–RanGppNHp complex with structure-based mapping of functional domains\",\n      \"pmids\": [\"10353245\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No co-crystal with a PY-NLS cargo was available\", \"Role of the HEAT-repeat 7 loop in substrate dissociation was inferred but not directly tested by mutagenesis in this study\"]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Mapping the PY-NLS of FUS as the transportin-binding element and showing that ALS-causing mutations within it impair nuclear import in proportion to clinical severity directly linked TNPO1-dependent transport to neurodegenerative disease pathogenesis.\",\n      \"evidence\": \"Nuclear import assays, co-immunoprecipitation, mutagenesis, live-cell imaging, siRNA knockdown of transportin, and immunofluorescence in patient tissue\",\n      \"pmids\": [\"20606625\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether restoring TNPO1-mediated import could rescue disease phenotypes in vivo was untested\", \"Contribution of stress-granule sequestration versus loss of nuclear function to neurodegeneration was unresolved\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Identification of a conserved PY-NLS in Ci/Gli transcription factors and demonstration that Sufu masks this signal to block TNPO1-mediated nuclear entry connected transportin to Hedgehog signaling and illustrated a regulatory strategy in which co-factors modulate import by NLS masking.\",\n      \"evidence\": \"PY-NLS mutagenesis, co-immunoprecipitation of Trn with Ci, genetic epistasis in Drosophila Hedgehog pathway, and mammalian Gli validation\",\n      \"pmids\": [\"24413177\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of Sufu masking of the PY-NLS was not determined\", \"Whether other signaling pathways regulate cargo access to TNPO1 by analogous masking was unknown\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Demonstrating that TNPO1 mediates nuclear import of LINE-1 ribonucleoprotein complexes and that miR-128 represses TNPO1 expression to restrict retrotransposition revealed a role for transportin in transposable element biology and a post-transcriptional regulatory layer controlling its abundance.\",\n      \"evidence\": \"TNPO1 knockdown/overexpression, L1 retrotransposition reporter assays, ORF1p nuclear import assays, and 3′ UTR luciferase reporters for miR-128 targeting\",\n      \"pmids\": [\"28974576\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct physical interaction between TNPO1 and L1-RNP was not demonstrated with purified components\", \"Whether TNPO1 recognizes a PY-NLS-like motif in L1 ORF1p or ORF2p was not mapped\", \"Findings from a single laboratory\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"A comprehensive structural picture of TNPO1 bound to its diverse PY-NLS cargoes (FUS, Gli, ribosomal proteins, L1-RNP) is still incomplete, and whether therapeutic modulation of TNPO1-mediated import can ameliorate ALS or other proteinopathies remains an open question.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No co-crystal structures with FUS, Gli, or ribosomal protein PY-NLS cargoes described in this timeline\", \"In vivo therapeutic relevance of restoring TNPO1-mediated FUS import in ALS models is untested\", \"Regulatory mechanisms controlling TNPO1 expression beyond miR-128 are uncharacterized\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005215\", \"supporting_discovery_ids\": [0, 3, 4, 5, 6]},\n      {\"term_id\": \"GO:0038024\", \"supporting_discovery_ids\": [0, 3, 4, 5]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0, 2, 3, 4, 5]},\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0, 4]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-9609507\", \"supporting_discovery_ids\": [0, 2, 3, 4, 5, 6]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"HNRNPA1\",\n      \"FUS\",\n      \"RAN\",\n      \"RPL23A\",\n      \"RPS7\",\n      \"RPL5\",\n      \"GLI2\",\n      \"SUFU\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```"}