{"gene":"NUP62","run_date":"2026-06-10T05:19:52","timeline":{"discoveries":[{"year":2007,"finding":"MUC1-C oncoprotein binds directly to the Nup62 central domain (and indirectly to the Nup62 C-terminal coiled-coil domain) for nuclear import; oligomerization via a CQC motif is required for Nup62 binding, and CQC→AQA mutation abrogates oligomerization, Nup62 binding, and nuclear localization of MUC1-C.","method":"Co-immunoprecipitation, direct binding assays with purified components, site-directed mutagenesis, stable expression of mutant constructs with nuclear localization readout","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1-2 / Moderate — direct binding with purified components, mutagenesis, and functional nuclear localization assay in single lab with multiple orthogonal methods","pmids":["17500061"],"is_preprint":false},{"year":2009,"finding":"The glucocorticoid receptor (GR)-hsp90 chaperone heterocomplex interacts with Nup62 at the nuclear pore to mediate GR nuclear import; GR cross-linked to the hsp90 heterocomplex can translocate to the nucleus in digitonin-permeabilized cells. FKBP52 and PP5 binding to Nup62 is hsp90-dependent, while hsp70 and p23 binding does not require hsp90.","method":"Co-immunoprecipitation, radicicol hsp90 inhibition, TPR peptide competition, digitonin-permeabilized cell nuclear transport assay","journal":"Molecular and cellular biology","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP with multiple components, chemical inhibitor validation, and functional transport assay in single lab","pmids":["19581287"],"is_preprint":false},{"year":2006,"finding":"A missense mutation in NUP62 (Q391P) causes autosomal recessive infantile bilateral striatal necrosis, demonstrating a cell-type-specific role for NUP62 in basal ganglia survival; Q391 is highly conserved across species.","method":"Genetic mapping, Sanger sequencing of candidate region, mutation co-segregation analysis across 8 families","journal":"Annals of neurology","confidence":"High","confidence_rationale":"Tier 2 / Strong — disease-causing mutation identified in multiple independent families, independently sequenced","pmids":["16786527"],"is_preprint":false},{"year":2010,"finding":"Human rhinovirus 2A protease (2Apro) directly cleaves NUP62 at multiple sites (between amino acids 103 and 298) in vitro, releasing the N-terminal FG-rich region from the nuclear pore complex in infected cells, thereby disrupting nucleocytoplasmic transport.","method":"In vitro cleavage assay with purified 2Apro and bacterially expressed Nup62, site-directed mutagenesis of cleavage sites, domain-specific antibodies in HRV/PV-infected cells","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1 / Moderate — reconstituted in vitro cleavage with purified components, mutagenesis of cleavage sites, confirmed in infected cells with domain-specific antibodies","pmids":["20622012"],"is_preprint":false},{"year":2017,"finding":"ROCK (Rho kinase) phosphorylates the FG regions of NUP62, reducing interaction between NUP62 and ΔNp63α and attenuating ΔNp63α nuclear import in squamous cell carcinoma cells; NUP62 depletion inhibits SCC cell proliferation and augments differentiation.","method":"siRNA knockdown, co-immunoprecipitation, phosphorylation assays, nuclear transport assays, differentiation/proliferation assays","journal":"EMBO reports","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP, kinase phosphorylation assay, functional KD with defined proliferation/differentiation phenotype, single lab","pmids":["29217659"],"is_preprint":false},{"year":2011,"finding":"β-Catenin directly interacts in vitro with the FG repeats of Nup62 via specific Armadillo (Arm) repeat sequences (R3-8 for import; R10-12 for import/export); Nup62 knockdown impedes the rate of β-catenin nuclear import/export to a greater extent than importin-β knockdown.","method":"FRAP in live cells, in vitro binding assay with purified components (direct interaction), siRNA knockdown, proteomics screen","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1-2 / Moderate — direct in vitro binding with purified components, FRAP functional assay, siRNA functional validation, single lab","pmids":["22110128"],"is_preprint":false},{"year":2011,"finding":"ORP8 (OSBP-related protein 8) interacts with Nup62 at the nuclear envelope, and ORP8's effects on nuclear SREBP levels and lipid homeostasis are inhibited when Nup62 is depleted, placing Nup62 downstream in ORP8-mediated SREBP regulation.","method":"Yeast two-hybrid, bimolecular fluorescence complementation (BiFC), co-immunoprecipitation, confocal immunofluorescence, siRNA knockdown epistasis","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2-3 / Moderate — multiple interaction methods (Y2H, BiFC, Co-IP) and functional epistasis, single lab","pmids":["21698267"],"is_preprint":false},{"year":2013,"finding":"NUP62 plays a role in centrosome integrity; RNAi depletion of Nup62 induces mitotic arrest in G2/M, defective centrosome segregation and centriole maturation, multinucleated cells, multipolar centrosomes, and spindle orientation defects, with impaired targeting of gamma-tubulin and SAS-6 to centrioles.","method":"RNAi knockdown, immunofluorescence microscopy, cell cycle analysis","journal":"Cell cycle (Georgetown, Tex.)","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — RNAi KD with defined centrosome and spindle phenotypes, multiple readouts, single lab","pmids":["24107630"],"is_preprint":false},{"year":2012,"finding":"HSV ICP27 directly binds Nup62 via sequences in both its N and C termini; this interaction is confirmed by co-immunoprecipitation and in vitro binding with purified components. ICP27 expression inhibits importin α/β-dependent and transportin-dependent nuclear import, but an ICP27 point mutant that does not interact with Nup62 lacks this inhibitory effect.","method":"Co-immunoprecipitation, in vitro binding with purified components, deletion and point mutagenesis, nuclear import assays","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1-2 / Moderate — direct in vitro binding with purified components, mutagenesis, functional import inhibition assay, single lab","pmids":["22334672"],"is_preprint":false},{"year":2022,"finding":"NUP62 is depleted from nuclei and mislocalizes to the cytoplasm in C9-ALS/FTLD iPSC neurons; cytoplasmic NUP62 interacts with TDP-43, promoting TDP-43 insolubility and inclusion formation. Poly-GR DPR accumulation triggers formation of cytoplasmic RNA granules that recruit both NUP62 and TDP-43. NUP62:TDP-43 inclusions are found in postmortem C9orf72 ALS/FTLD and sporadic ALS/FTLD CNS tissue.","method":"iPSC neuron models, co-immunoprecipitation/co-localization, solubility fractionation, postmortem tissue immunostaining","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (Co-IP, fractionation, live iPSC neurons, postmortem tissue), replicated in disease tissue","pmids":["35697676"],"is_preprint":false},{"year":2014,"finding":"Phosphorylation of NUP62 at a FAK/PYK2 consensus site (human Y422/rat Y425) by PYK2 is associated with shedding of NUP62 from the nuclear pore complex and/or retention in the cytoplasm. Depletion of Nup62 from hippocampal and cortical neurons causes simplification and retraction of dendritic arbors without disrupting axon initial segment integrity.","method":"Phosphorylation assay in cultured cells, fractionation, immunofluorescence in chronically stressed rat hippocampus, RNAi knockdown in primary neurons with morphological readout","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"Medium","confidence_rationale":"Tier 2-3 / Moderate — phosphorylation identified in cells, functional KD in primary neurons with morphological phenotype, in vivo stressed animal, single lab","pmids":["25349423"],"is_preprint":false},{"year":2009,"finding":"Nup62 directly interacts with Exo70 via its coiled-coil domain (not the FG-repeat domain) and colocalizes with Exo70 at the leading edge of migrating cells; Exo70 recruits Nup62 to the plasma membrane and filopodia. siRNA knockdown of Nup62 at the leading edge significantly reduces cell migration.","method":"Direct binding assay, co-immunoprecipitation, confocal microscopy, siRNA knockdown, cell migration assay","journal":"Traffic (Copenhagen, Denmark)","confidence":"High","confidence_rationale":"Tier 1-2 / Moderate — direct binding assay, Co-IP, functional KD with migration phenotype, domain-deletion mapping, single lab","pmids":["19552648"],"is_preprint":false},{"year":2015,"finding":"Nup62, Nup54, and Nup58 form a dynamic triple complex in solution via their ordered (α-helical) regions; Nup54 acts as a bridge connecting Nup62 and Nup58 through two distinct cognate segment interactions. The stoichiometry of 4:2:1 (Nup62:Nup54:Nup58) inferred from crystal structures is confirmed by solution analysis.","method":"Size exclusion chromatography, solution biophysics (SEC-MALS, analytical ultracentrifugation implied), crystal structure analysis","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1 / Moderate — crystal structures plus solution biophysical analysis, confirms stoichiometry and dynamic complex formation","pmids":["26025361"],"is_preprint":false},{"year":2017,"finding":"The crystal structure of the rat Nup62 coiled-coil domain (residues 362-425) at 2.4 Å resolution reveals a parallel three-helix bundle; in solution it exists as homodimer or homotrimer. The coiled-coil domain of Nup62 is sufficient for interaction with the coiled-coil domain of Exo70, demonstrating a chain replacement mechanism enabling diverse protein assemblies.","method":"X-ray crystallography (2.4 Å), SEC-MALS, glutaraldehyde cross-linking, in vitro binding assay","journal":"Biochemistry","confidence":"High","confidence_rationale":"Tier 1 / Moderate — crystal structure with solution validation and in vitro domain binding, single lab","pmids":["28406021"],"is_preprint":false},{"year":2022,"finding":"TIP60 acetyltransferase acetylates Nup62 at Lys432 during mitotic entry, dissolving the Nup62-Nup58-Nup54 nucleoporin complex and redistributing Nup62 to the mitotic spindle; this acetylation-driven remodeling is required for correct spindle orientation and accurate chromosome segregation.","method":"In vitro acetylation assay, mutagenesis (acetylation-mimetic/defective mutants), immunofluorescence, siRNA knockdown with spindle/chromosome segregation readouts","journal":"Journal of molecular cell biology","confidence":"High","confidence_rationale":"Tier 1-2 / Moderate — in vitro acetyltransferase assay, mutagenesis of acetylation site, functional spindle/segregation phenotype, single lab","pmids":["36190325"],"is_preprint":false},{"year":2020,"finding":"NUP62 depletion causes defective spindle assembly checkpoint (SAC); depletion causes slight decrease in MAD2 protein levels after nocodazole but does not affect kinetochore localization of BUBR1, MAD1, or MAD2. NUP62 depletion in neural stem cells induces aneuploidy. Overexpression of the disease mutant NUP62(Q391P) also causes SAC defects, indicating Q391 is critical for SAC function.","method":"siRNA knockdown, overexpression of Q391P mutant, mitotic timing analysis, immunofluorescence for SAC components, aneuploidy assay in neural stem cells","journal":"The international journal of biochemistry & cell biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — KD with defined SAC phenotype, mutant overexpression, multiple cell types, single lab","pmids":["32905854"],"is_preprint":false},{"year":2020,"finding":"In Drosophila premeiotic spermatocytes, Cyclin B (CycB) forms a protein complex with Exportin (Emb) and Nup62; CycB must be exported from the nucleus via this complex (interacting with Nup62 channel subcomplex) to enable CDK1 activation and meiotic entry. Depletion of Nup62 traps CycB in nuclei and blocks CDK1 activation; ectopic CycB overexpression partially rescues the meiotic block.","method":"dsRNA-mediated knockdown (Gal4/UAS), co-immunoprecipitation of CycB-Emb-Nup62 complex, rescue experiments with CycB/active CDK1 overexpression, fluorescence imaging","journal":"Cells","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Co-IP of ternary complex, genetic KD with rescue, Drosophila model, single lab","pmids":["31979075"],"is_preprint":false},{"year":2016,"finding":"Nup62 associates with mitotic spindle microtubules (not spindle matrix); its spindle localization depends on its three coiled-coil domains, not on CRM1 (though Nup62 interacts with CRM1 during mitosis). Nup62 knockdown causes defects in chromosome alignment and spindle assembly, with polar chromosome congression defects in >30% of depleted cells.","method":"RNAi knockdown, immunofluorescence, domain deletion analysis, spindle association fractionation","journal":"Cell biology international","confidence":"Medium","confidence_rationale":"Tier 2-3 / Moderate — KD with defined mitotic phenotype, domain mapping for spindle localization, single lab","pmids":["27298184"],"is_preprint":false},{"year":2013,"finding":"Nuclear import of HPV16 E7 oncoprotein is mediated via hydrophobic interactions between a patch of residues (65LRLCV69) in the E7 zinc-binding domain and the FG domain of Nup62; an intact zinc-binding domain and specific cysteine residues are required for this importin-independent nuclear import pathway.","method":"Mutagenesis of cysteine and hydrophobic residues, EGFP-fusion nuclear localization assays, functional import analysis","journal":"Virology","confidence":"Medium","confidence_rationale":"Tier 2-3 / Moderate — mutagenesis with nuclear localization readout, single lab, mechanism inferred from localization changes","pmids":["24074597"],"is_preprint":false},{"year":2023,"finding":"NUP62 overexpression stabilizes NUP88 by inhibiting proteasome-mediated degradation of Nup88; the Nup88-Nup62 interaction is independent of Nup glycosylation status and cell-cycle stage. Stabilized Nup88 interacts with NF-κB (p65) and partially sequesters it into the nucleus of unstimulated cells, inducing NF-κB target genes (Akt, c-myc, IL-6, BIRC3).","method":"Co-immunoprecipitation, proteasome inhibitor experiments, siRNA knockdown, NF-κB target gene expression analysis, patient sample validation","journal":"Frontiers in oncology","confidence":"Medium","confidence_rationale":"Tier 2-3 / Moderate — Co-IP, proteasome inhibition showing Nup62-dependent Nup88 stability, functional NF-κB pathway output, single lab","pmids":["36845732"],"is_preprint":false},{"year":2023,"finding":"The structured C-terminal coiled-coil domain of Nup62 (not its N-terminal FG-repeat domain) is the dominant determinant for binding FUS and inducing co-phase separation of FUS/Nup62 into amorphous assemblies; expression of isolated C-terminal domain in human cells is sufficient for nuclear envelope localization.","method":"In vitro phase separation assay with recombinant proteins, domain deletion analysis, biochemical binding assays, fluorescence microscopy in human cells","journal":"Journal of molecular biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reconstituted in vitro with recombinant proteins, domain mapping, cellular localization validation, single lab","pmids":["36690069"],"is_preprint":false},{"year":2025,"finding":"NUP62 promotes nuclear transport of the transcription factor E2F1, which in turn stimulates transcription of the epigenetic enzyme NSD2; NSD2-dependent H3K36me2/H3K36me3 modifications of anti-aging genes (HMGA1, HMGA2, SIRT6) mediate NUP62's role in alleviating senescence in dental pulp stem cells.","method":"RNA-seq, epigenomic landscape analysis, NUP62 overexpression/knockdown, nuclear transport assay for E2F1, in vitro and in vivo differentiation assays","journal":"International journal of oral science","confidence":"Medium","confidence_rationale":"Tier 2-3 / Moderate — functional KD/OE with pathway placement via E2F1 nuclear transport and NSD2 epigenetics, single lab","pmids":["40246825"],"is_preprint":false},{"year":2026,"finding":"NUP62 competitively binds KEAP1, preventing KEAP1-mediated ubiquitination and degradation of NRF2; this stabilizes NRF2 and promotes its nuclear translocation, enhancing transcription of antioxidant genes and inhibiting ferroptosis in breast cancer cells.","method":"Co-immunoprecipitation, ubiquitination assay, NRF2 stability/nuclear localization assay, siRNA knockdown, xenograft in vivo model","journal":"iScience","confidence":"Medium","confidence_rationale":"Tier 2-3 / Moderate — Co-IP, ubiquitination assay, functional NRF2 localization and target gene readout, single lab","pmids":["42016308"],"is_preprint":false},{"year":2026,"finding":"NUP62 knockdown reduces survivin protein levels through the ubiquitin-proteasome system (enhanced ubiquitination and shortened protein half-life); survivin downregulation mediates NUP62-knockdown-induced apoptosis via caspase-3 activation in osimertinib-resistant NSCLC cells.","method":"siRNA knockdown, ubiquitination assay, cycloheximide chase (protein half-life), caspase-3 activity assay, survivin overexpression rescue, xenograft in vivo","journal":"British journal of cancer","confidence":"Medium","confidence_rationale":"Tier 2-3 / Moderate — ubiquitination assay, protein stability measurement, rescue experiment, single lab","pmids":["42185638"],"is_preprint":false},{"year":2012,"finding":"NUP62 and NUP214 are differentially distributed between nuclear pore complexes on flattened nuclear surfaces and the peripheral rim, indicating architectural heterogeneity among NPC populations in adherent cells.","method":"STED super-resolution immunofluorescence microscopy, orthogonal imaging of cell nuclei","journal":"PloS one","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single imaging-based localization study, no functional consequence tested, single lab","pmids":["22558357"],"is_preprint":false},{"year":2020,"finding":"Reduction of Nup62 content enhances density-induced myoblast differentiation in high-mitogen medium, while forced Nup62 expression inhibits density-induced differentiation; this effect involves p38 MAP kinase activation. Differentiation induced by low-mitogen medium is unaffected by ectopic Nup62 expression.","method":"siRNA knockdown, ectopic overexpression, differentiation assay, p38 MAP kinase activation readout in C2C12 myoblasts","journal":"Differentiation; research in biological diversity","confidence":"Low","confidence_rationale":"Tier 3 / Weak — KD/OE with differentiation phenotype, p38 pathway involvement shown but mechanism not fully characterized, single lab","pmids":["32554220"],"is_preprint":false},{"year":2025,"finding":"During post-mitotic NPC assembly, degrading Nup62 arrests assembly at an intermediate step with smaller membrane pores and removes the whole central transport channel; 32 copies of the central channel subcomplex self-associate via hydrophobic interactions to occupy the pore center and exert an outward pushing force for full pore dilation. Disrupting these hydrophobic interactions during assembly blocked pore dilation, impaired nuclear import, and caused smaller nuclei and looser NE spacing.","method":"Acute molecular perturbations in live cells combined with correlative 3D electron tomography and MINFLUX super-resolution microscopy, molecular dynamics simulations","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 1-2 / Moderate — structural imaging (ET + MINFLUX), live-cell perturbation, MD simulations; preprint not yet peer-reviewed","pmids":[],"is_preprint":true}],"current_model":"NUP62 is a central channel nucleoporin that forms a dynamic heterocomplex with Nup54 and Nup58 (via coiled-coil interactions) to build the NPC transport channel, directly mediates nuclear import of diverse cargos (including MUC1-C, GR-hsp90, β-catenin, ΔNp63α, and viral proteins) through FG-repeat and coiled-coil domain interactions, undergoes regulatory post-translational modifications (TIP60-mediated acetylation at K432 during mitosis to remodel the Nup62 complex and direct spindle orientation; PYK2-mediated phosphorylation at Y422 to release it from the NPC), and has non-canonical roles at the mitotic spindle (chromosome alignment, SAC maintenance), at the leading edge of migrating cells (via Exo70 interaction), and in pathological contexts including ALS/FTLD (cytoplasmic mislocalization promotes TDP-43 insolubility) and viral infection (2A protease cleavage of FG-repeat domain disrupts nucleocytoplasmic transport)."},"narrative":{"mechanistic_narrative":"NUP62 is a central-channel nucleoporin that builds the transport conduit of the nuclear pore complex and serves as a hub for both classical and importin-independent nuclear translocation of diverse cargos [PMID:22110128, PMID:26025361]. Structurally, it forms a dynamic triple complex with Nup54 and Nup58 in which Nup54 bridges the two partners through its ordered α-helical regions, assembling at a 4:2:1 stoichiometry; its C-terminal segment adopts a parallel three-helix coiled-coil bundle [PMID:26025361, PMID:28406021]. During post-mitotic NPC assembly, self-association of many copies of this central-channel subcomplex via hydrophobic interactions occupies and dilates the pore, and loss of NUP62 arrests assembly with smaller pores and impaired import. The protein engages cargo through two functionally distinct modules: its FG-repeat region binds substrates such as β-catenin, ΔNp63α, and viral oncoproteins (HPV16 E7), while its structured coiled-coil domain mediates partner interactions including Exo70 and FUS [PMID:22110128, PMID:29217659, PMID:24074597, PMID:19552648, PMID:36690069]. NUP62 thereby controls nuclear import of multiple signaling and oncogenic factors—the MUC1-C oncoprotein, the GR-hsp90 chaperone heterocomplex, β-catenin, and ΔNp63α [PMID:17500061, PMID:19581287, PMID:22110128, PMID:29217659]. Beyond the pore, NUP62 has non-canonical roles: TIP60-mediated acetylation at Lys432 dissolves the Nup62–Nup58–Nup54 complex at mitotic entry and redirects NUP62 to the mitotic spindle to control spindle orientation and chromosome segregation, and NUP62 is independently required for centrosome integrity, spindle-assembly-checkpoint function, and chromosome alignment [PMID:36190325, PMID:24107630, PMID:32905854, PMID:27298184]. At the leading edge of migrating cells it is recruited to the plasma membrane by Exo70 via its coiled-coil domain to promote migration [PMID:19552648]. A recessive Q391P missense mutation in NUP62 causes infantile bilateral striatal necrosis, and the same residue is critical for spindle-checkpoint function [PMID:16786527, PMID:32905854]. In ALS/FTLD, NUP62 mislocalizes to the cytoplasm where it binds TDP-43 and promotes its insolubility and inclusion formation [PMID:35697676]. NUP62 activity is regulated by post-translational modification, including ROCK and PYK2 phosphorylation of its FG/Y422 regions, the latter releasing it from the pore [PMID:29217659, PMID:25349423].","teleology":[{"year":2006,"claim":"Established that NUP62 has a non-redundant, cell-type-specific physiological requirement, linking this nucleoporin to a defined human disease.","evidence":"Genetic mapping and Sanger sequencing of a Q391P missense mutation co-segregating across 8 families with infantile bilateral striatal necrosis","pmids":["16786527"],"confidence":"High","gaps":["Does not explain why basal ganglia neurons are selectively vulnerable","Molecular consequence of Q391P on NPC function not resolved here"]},{"year":2007,"claim":"Showed NUP62 acts as a direct import receptor for an oncogenic cargo, defining a binding mechanism dependent on cargo oligomerization.","evidence":"Co-IP, direct binding with purified components, and CQC-motif mutagenesis abolishing MUC1-C oligomerization, Nup62 binding, and nuclear localization","pmids":["17500061"],"confidence":"High","gaps":["Whether import is importin-independent not established","Did not map the precise FG vs coiled-coil contribution to cargo affinity"]},{"year":2009,"claim":"Extended the cargo repertoire to a chaperoned receptor complex and to the actin-cytoskeleton/migration machinery, revealing NUP62 functions beyond the central channel.","evidence":"Digitonin-permeabilized transport assays with the GR-hsp90 heterocomplex; direct binding and domain-deletion mapping of Exo70 to the coiled-coil domain with migration knockdown","pmids":["19581287","19552648"],"confidence":"High","gaps":["Stoichiometry of GR-hsp90 docking on NUP62 not defined","How the same coiled-coil serves both NPC assembly and leading-edge recruitment unclear"]},{"year":2010,"claim":"Demonstrated that pathogens disable nucleocytoplasmic transport by directly proteolyzing NUP62, defining its FG region as a viral target.","evidence":"In vitro cleavage of bacterially expressed Nup62 by purified rhinovirus 2A protease, cleavage-site mutagenesis, and domain-specific antibodies in infected cells","pmids":["20622012"],"confidence":"High","gaps":["Quantitative contribution of NUP62 cleavage versus other nucleoporins to transport collapse not isolated"]},{"year":2011,"claim":"Resolved cargo-specific binding determinants, showing the FG repeats engage β-catenin Arm repeats and that NUP62 rate-limits its bidirectional transport.","evidence":"FRAP in live cells, in vitro binding with purified components mapping Arm repeats R3-8/R10-12, and siRNA knockdown comparison with importin-β; separate Y2H/BiFC/Co-IP placing NUP62 downstream of ORP8 in SREBP regulation","pmids":["22110128","21698267"],"confidence":"High","gaps":["ORP8 epistasis is Medium-confidence and lacks reconstitution","Whether β-catenin transport is fully importin-independent not settled"]},{"year":2013,"claim":"Uncovered a non-canonical mitotic role at centrosomes and added a viral cargo using importin-independent FG binding.","evidence":"RNAi depletion producing centrosome segregation, centriole maturation, and spindle-orientation defects; mutagenesis mapping HPV16 E7 zinc-binding-domain residues to the FG domain","pmids":["24107630","24074597"],"confidence":"Medium","gaps":["Centrosome phenotype could be indirect via global transport defects","E7 import mechanism inferred from localization, not direct flux measurement"]},{"year":2012,"claim":"Identified ICP27 as a viral inhibitor that hijacks NUP62 binding to block both importin and transportin pathways.","evidence":"Co-IP and in vitro binding with purified components, point mutagenesis of ICP27, and import inhibition assays","pmids":["22334672"],"confidence":"High","gaps":["Mechanism by which ICP27-NUP62 binding blocks multiple receptor pathways not defined"]},{"year":2014,"claim":"Defined phosphoregulation that releases NUP62 from the pore and linked it to neuronal architecture.","evidence":"PYK2 phosphorylation at Y422/Y425 with fractionation showing NPC shedding; RNAi in primary neurons causing dendritic retraction; in vivo stressed hippocampus","pmids":["25349423"],"confidence":"Medium","gaps":["Causal link between Y422 phosphorylation and dendritic phenotype not directly tested","Single lab"]},{"year":2015,"claim":"Provided the structural basis for the central-channel heterocomplex, defining Nup54 as the bridging subunit and the 4:2:1 stoichiometry.","evidence":"Crystal structures plus solution biophysics (SEC, SEC-MALS) of the Nup62-Nup54-Nup58 ordered regions","pmids":["26025361"],"confidence":"High","gaps":["Does not show how the assembled complex behaves within an intact pore"]},{"year":2016,"claim":"Localized NUP62 to spindle microtubules and showed its coiled-coil domains, not FG repeats or CRM1, drive spindle targeting and chromosome alignment.","evidence":"RNAi knockdown, immunofluorescence, domain-deletion analysis, and spindle fractionation","pmids":["27298184"],"confidence":"Medium","gaps":["Direct microtubule-binding partner on the spindle not identified","Single lab"]},{"year":2017,"claim":"Solved the coiled-coil structure and demonstrated a chain-replacement mechanism enabling NUP62 to switch between NPC and non-NPC partners; ROCK phosphorylation tunes ΔNp63α import in cancer.","evidence":"2.4 Å crystal structure, SEC-MALS, cross-linking, and in vitro Exo70 binding; siRNA/Co-IP/phosphorylation and proliferation-differentiation assays in SCC","pmids":["28406021","29217659"],"confidence":"High","gaps":["In vivo relevance of homo- versus hetero-oligomer switching not established"]},{"year":2020,"claim":"Connected NUP62 to spindle-assembly-checkpoint fidelity and meiotic cell-cycle progression, with the disease residue Q391 implicated in checkpoint function.","evidence":"siRNA knockdown and Q391P overexpression with SAC and aneuploidy readouts; Drosophila Co-IP of a CycB-Emb-Nup62 export complex with knockdown and rescue","pmids":["32905854","31979075"],"confidence":"Medium","gaps":["Mechanism linking Q391 to SAC not resolved","CycB export role demonstrated in Drosophila, human conservation untested"]},{"year":2022,"claim":"Defined acetylation as a mitotic switch remodeling the NUP62 complex and revealed a pathological cytoplasmic gain-of-function in neurodegeneration.","evidence":"In vitro TIP60 acetylation, K432 acetyl-mimetic/defective mutants with spindle/segregation readouts; iPSC neuron models, Co-IP/fractionation, and postmortem ALS/FTLD tissue showing NUP62:TDP-43 inclusions","pmids":["36190325","35697676"],"confidence":"High","gaps":["How K432 acetylation directs spindle targeting mechanistically unclear","Whether NUP62 mislocalization is cause or consequence of TDP-43 pathology not resolved"]},{"year":2023,"claim":"Established that the structured C-terminal domain, not the FG region, drives phase separation with FUS and that NUP62 stabilizes other nucleoporins to influence signaling output.","evidence":"In vitro phase separation with recombinant FUS/Nup62 and domain mapping; Co-IP and proteasome-inhibition experiments showing Nup62-dependent Nup88 stabilization and NF-κB activation","pmids":["36690069","36845732"],"confidence":"Medium","gaps":["Physiological role of FUS/NUP62 co-phase separation not defined","Nup88/NF-κB axis from single lab"]},{"year":2025,"claim":"Placed NUP62 upstream of transcriptional and epigenetic programs governing senescence and antioxidant defense via cargo-specific transport.","evidence":"RNA-seq/epigenomics with NUP62 OE/KD and E2F1 nuclear-transport assays linking to NSD2 anti-aging genes; Co-IP/ubiquitination assays placing NUP62 as a KEAP1 competitor stabilizing NRF2","pmids":["40246825","42016308"],"confidence":"Medium","gaps":["Whether E2F1 and NRF2 effects are direct transport functions or indirect not fully separated","Single lab per pathway"]},{"year":2026,"claim":"Linked NUP62 to apoptotic control in drug-resistant cancer through proteostatic regulation of survivin.","evidence":"siRNA knockdown, ubiquitination assay, cycloheximide chase, caspase-3 assay, survivin rescue, and xenograft in osimertinib-resistant NSCLC","pmids":["42185638"],"confidence":"Medium","gaps":["Direct versus indirect mechanism by which NUP62 controls survivin stability unclear","Single context (resistant NSCLC)"]},{"year":null,"claim":"How NUP62's mitotic, leading-edge, transcriptional, and proteostatic functions are coordinated with its core channel role, and which functions are direct versus secondary to global transport changes, remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No unified model distinguishing on-pore from off-pore activities","Most non-canonical roles rest on single-lab studies","In vivo significance of post-translational switches beyond mitosis unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140104","term_label":"molecular carrier activity","supporting_discovery_ids":[0,1,5,4,18]},{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[12,13,26]},{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[17]},{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[19,22,23]}],"localization":[{"term_id":"GO:0005635","term_label":"nuclear envelope","supporting_discovery_ids":[12,24,6,20]},{"term_id":"GO:0005815","term_label":"microtubule organizing center","supporting_discovery_ids":[7]},{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[17,14]},{"term_id":"GO:0005886","term_label":"plasma membrane","supporting_discovery_ids":[11]},{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[9,10]}],"pathway":[{"term_id":"R-HSA-9609507","term_label":"Protein localization","supporting_discovery_ids":[0,1,5,12,26]},{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[7,14,15,17]},{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[4,19,22]},{"term_id":"R-HSA-1643685","term_label":"Disease","supporting_discovery_ids":[2,9]}],"complexes":["Nup62-Nup54-Nup58 central channel subcomplex","nuclear pore complex"],"partners":["NUP54","NUP58","EXOC7","FUS","NUP88","CTNNB1","KEAP1","TARDBP"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P37198","full_name":"Nuclear pore glycoprotein p62","aliases":["62 kDa nucleoporin","Nucleoporin Nup62"],"length_aa":522,"mass_kda":53.3,"function":"Essential component of the nuclear pore complex (PubMed:1915414). The N-terminal is probably involved in nucleocytoplasmic transport (PubMed:1915414). The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex (PubMed:1915414, PubMed:24107630). Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation (PubMed:24107630). It might be involved in protein recruitment to the centrosome after nuclear breakdown (PubMed:24107630)","subcellular_location":"Nucleus, nuclear pore complex; Cytoplasm, cytoskeleton, spindle pole; Nucleus envelope; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome","url":"https://www.uniprot.org/uniprotkb/P37198/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/NUP62","classification":"Common 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NUP93","url":"https://www.omim.org/entry/614351"},{"mim_id":"611729","title":"KINESIN LIGHT CHAIN 2; KLC2","url":"https://www.omim.org/entry/611729"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Nuclear membrane","reliability":"Supported"},{"location":"Nucleoplasm","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/NUP62"},"hgnc":{"alias_symbol":["p62","DKFZp547L134","IBSN","SNDI","MGC841","FLJ20822","FLJ43869"],"prev_symbol":[]},"alphafold":{"accession":"P37198","domains":[{"cath_id":"1.20.5","chopping":"333-422","consensus_level":"medium","plddt":91.3999,"start":333,"end":422},{"cath_id":"1.20.5","chopping":"430-461","consensus_level":"medium","plddt":88.8388,"start":430,"end":461},{"cath_id":"1.20.5","chopping":"469-522","consensus_level":"medium","plddt":86.1117,"start":469,"end":522}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P37198","model_url":"https://alphafold.ebi.ac.uk/files/AF-P37198-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P37198-F1-predicted_aligned_error_v6.png","plddt_mean":57.91},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=NUP62","jax_strain_url":"https://www.jax.org/strain/search?query=NUP62"},"sequence":{"accession":"P37198","fasta_url":"https://rest.uniprot.org/uniprotkb/P37198.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P37198/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P37198"}},"corpus_meta":[{"pmid":"17500061","id":"PMC_17500061","title":"Nuclear 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\"Co-immunoprecipitation, direct binding assays with purified components, site-directed mutagenesis, stable expression of mutant constructs with nuclear localization readout\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — direct binding with purified components, mutagenesis, and functional nuclear localization assay in single lab with multiple orthogonal methods\",\n      \"pmids\": [\"17500061\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"The glucocorticoid receptor (GR)-hsp90 chaperone heterocomplex interacts with Nup62 at the nuclear pore to mediate GR nuclear import; GR cross-linked to the hsp90 heterocomplex can translocate to the nucleus in digitonin-permeabilized cells. FKBP52 and PP5 binding to Nup62 is hsp90-dependent, while hsp70 and p23 binding does not require hsp90.\",\n      \"method\": \"Co-immunoprecipitation, radicicol hsp90 inhibition, TPR peptide competition, digitonin-permeabilized cell nuclear transport assay\",\n      \"journal\": \"Molecular and cellular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP with multiple components, chemical inhibitor validation, and functional transport assay in single lab\",\n      \"pmids\": [\"19581287\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2006,\n      \"finding\": \"A missense mutation in NUP62 (Q391P) causes autosomal recessive infantile bilateral striatal necrosis, demonstrating a cell-type-specific role for NUP62 in basal ganglia survival; Q391 is highly conserved across species.\",\n      \"method\": \"Genetic mapping, Sanger sequencing of candidate region, mutation co-segregation analysis across 8 families\",\n      \"journal\": \"Annals of neurology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — disease-causing mutation identified in multiple independent families, independently sequenced\",\n      \"pmids\": [\"16786527\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"Human rhinovirus 2A protease (2Apro) directly cleaves NUP62 at multiple sites (between amino acids 103 and 298) in vitro, releasing the N-terminal FG-rich region from the nuclear pore complex in infected cells, thereby disrupting nucleocytoplasmic transport.\",\n      \"method\": \"In vitro cleavage assay with purified 2Apro and bacterially expressed Nup62, site-directed mutagenesis of cleavage sites, domain-specific antibodies in HRV/PV-infected cells\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — reconstituted in vitro cleavage with purified components, mutagenesis of cleavage sites, confirmed in infected cells with domain-specific antibodies\",\n      \"pmids\": [\"20622012\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"ROCK (Rho kinase) phosphorylates the FG regions of NUP62, reducing interaction between NUP62 and ΔNp63α and attenuating ΔNp63α nuclear import in squamous cell carcinoma cells; NUP62 depletion inhibits SCC cell proliferation and augments differentiation.\",\n      \"method\": \"siRNA knockdown, co-immunoprecipitation, phosphorylation assays, nuclear transport assays, differentiation/proliferation assays\",\n      \"journal\": \"EMBO reports\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP, kinase phosphorylation assay, functional KD with defined proliferation/differentiation phenotype, single lab\",\n      \"pmids\": [\"29217659\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"β-Catenin directly interacts in vitro with the FG repeats of Nup62 via specific Armadillo (Arm) repeat sequences (R3-8 for import; R10-12 for import/export); Nup62 knockdown impedes the rate of β-catenin nuclear import/export to a greater extent than importin-β knockdown.\",\n      \"method\": \"FRAP in live cells, in vitro binding assay with purified components (direct interaction), siRNA knockdown, proteomics screen\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — direct in vitro binding with purified components, FRAP functional assay, siRNA functional validation, single lab\",\n      \"pmids\": [\"22110128\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"ORP8 (OSBP-related protein 8) interacts with Nup62 at the nuclear envelope, and ORP8's effects on nuclear SREBP levels and lipid homeostasis are inhibited when Nup62 is depleted, placing Nup62 downstream in ORP8-mediated SREBP regulation.\",\n      \"method\": \"Yeast two-hybrid, bimolecular fluorescence complementation (BiFC), co-immunoprecipitation, confocal immunofluorescence, siRNA knockdown epistasis\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 / Moderate — multiple interaction methods (Y2H, BiFC, Co-IP) and functional epistasis, single lab\",\n      \"pmids\": [\"21698267\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"NUP62 plays a role in centrosome integrity; RNAi depletion of Nup62 induces mitotic arrest in G2/M, defective centrosome segregation and centriole maturation, multinucleated cells, multipolar centrosomes, and spindle orientation defects, with impaired targeting of gamma-tubulin and SAS-6 to centrioles.\",\n      \"method\": \"RNAi knockdown, immunofluorescence microscopy, cell cycle analysis\",\n      \"journal\": \"Cell cycle (Georgetown, Tex.)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — RNAi KD with defined centrosome and spindle phenotypes, multiple readouts, single lab\",\n      \"pmids\": [\"24107630\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"HSV ICP27 directly binds Nup62 via sequences in both its N and C termini; this interaction is confirmed by co-immunoprecipitation and in vitro binding with purified components. ICP27 expression inhibits importin α/β-dependent and transportin-dependent nuclear import, but an ICP27 point mutant that does not interact with Nup62 lacks this inhibitory effect.\",\n      \"method\": \"Co-immunoprecipitation, in vitro binding with purified components, deletion and point mutagenesis, nuclear import assays\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — direct in vitro binding with purified components, mutagenesis, functional import inhibition assay, single lab\",\n      \"pmids\": [\"22334672\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"NUP62 is depleted from nuclei and mislocalizes to the cytoplasm in C9-ALS/FTLD iPSC neurons; cytoplasmic NUP62 interacts with TDP-43, promoting TDP-43 insolubility and inclusion formation. Poly-GR DPR accumulation triggers formation of cytoplasmic RNA granules that recruit both NUP62 and TDP-43. NUP62:TDP-43 inclusions are found in postmortem C9orf72 ALS/FTLD and sporadic ALS/FTLD CNS tissue.\",\n      \"method\": \"iPSC neuron models, co-immunoprecipitation/co-localization, solubility fractionation, postmortem tissue immunostaining\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (Co-IP, fractionation, live iPSC neurons, postmortem tissue), replicated in disease tissue\",\n      \"pmids\": [\"35697676\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"Phosphorylation of NUP62 at a FAK/PYK2 consensus site (human Y422/rat Y425) by PYK2 is associated with shedding of NUP62 from the nuclear pore complex and/or retention in the cytoplasm. Depletion of Nup62 from hippocampal and cortical neurons causes simplification and retraction of dendritic arbors without disrupting axon initial segment integrity.\",\n      \"method\": \"Phosphorylation assay in cultured cells, fractionation, immunofluorescence in chronically stressed rat hippocampus, RNAi knockdown in primary neurons with morphological readout\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 / Moderate — phosphorylation identified in cells, functional KD in primary neurons with morphological phenotype, in vivo stressed animal, single lab\",\n      \"pmids\": [\"25349423\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"Nup62 directly interacts with Exo70 via its coiled-coil domain (not the FG-repeat domain) and colocalizes with Exo70 at the leading edge of migrating cells; Exo70 recruits Nup62 to the plasma membrane and filopodia. siRNA knockdown of Nup62 at the leading edge significantly reduces cell migration.\",\n      \"method\": \"Direct binding assay, co-immunoprecipitation, confocal microscopy, siRNA knockdown, cell migration assay\",\n      \"journal\": \"Traffic (Copenhagen, Denmark)\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — direct binding assay, Co-IP, functional KD with migration phenotype, domain-deletion mapping, single lab\",\n      \"pmids\": [\"19552648\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Nup62, Nup54, and Nup58 form a dynamic triple complex in solution via their ordered (α-helical) regions; Nup54 acts as a bridge connecting Nup62 and Nup58 through two distinct cognate segment interactions. The stoichiometry of 4:2:1 (Nup62:Nup54:Nup58) inferred from crystal structures is confirmed by solution analysis.\",\n      \"method\": \"Size exclusion chromatography, solution biophysics (SEC-MALS, analytical ultracentrifugation implied), crystal structure analysis\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — crystal structures plus solution biophysical analysis, confirms stoichiometry and dynamic complex formation\",\n      \"pmids\": [\"26025361\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"The crystal structure of the rat Nup62 coiled-coil domain (residues 362-425) at 2.4 Å resolution reveals a parallel three-helix bundle; in solution it exists as homodimer or homotrimer. The coiled-coil domain of Nup62 is sufficient for interaction with the coiled-coil domain of Exo70, demonstrating a chain replacement mechanism enabling diverse protein assemblies.\",\n      \"method\": \"X-ray crystallography (2.4 Å), SEC-MALS, glutaraldehyde cross-linking, in vitro binding assay\",\n      \"journal\": \"Biochemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — crystal structure with solution validation and in vitro domain binding, single lab\",\n      \"pmids\": [\"28406021\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"TIP60 acetyltransferase acetylates Nup62 at Lys432 during mitotic entry, dissolving the Nup62-Nup58-Nup54 nucleoporin complex and redistributing Nup62 to the mitotic spindle; this acetylation-driven remodeling is required for correct spindle orientation and accurate chromosome segregation.\",\n      \"method\": \"In vitro acetylation assay, mutagenesis (acetylation-mimetic/defective mutants), immunofluorescence, siRNA knockdown with spindle/chromosome segregation readouts\",\n      \"journal\": \"Journal of molecular cell biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — in vitro acetyltransferase assay, mutagenesis of acetylation site, functional spindle/segregation phenotype, single lab\",\n      \"pmids\": [\"36190325\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"NUP62 depletion causes defective spindle assembly checkpoint (SAC); depletion causes slight decrease in MAD2 protein levels after nocodazole but does not affect kinetochore localization of BUBR1, MAD1, or MAD2. NUP62 depletion in neural stem cells induces aneuploidy. Overexpression of the disease mutant NUP62(Q391P) also causes SAC defects, indicating Q391 is critical for SAC function.\",\n      \"method\": \"siRNA knockdown, overexpression of Q391P mutant, mitotic timing analysis, immunofluorescence for SAC components, aneuploidy assay in neural stem cells\",\n      \"journal\": \"The international journal of biochemistry & cell biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — KD with defined SAC phenotype, mutant overexpression, multiple cell types, single lab\",\n      \"pmids\": [\"32905854\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"In Drosophila premeiotic spermatocytes, Cyclin B (CycB) forms a protein complex with Exportin (Emb) and Nup62; CycB must be exported from the nucleus via this complex (interacting with Nup62 channel subcomplex) to enable CDK1 activation and meiotic entry. Depletion of Nup62 traps CycB in nuclei and blocks CDK1 activation; ectopic CycB overexpression partially rescues the meiotic block.\",\n      \"method\": \"dsRNA-mediated knockdown (Gal4/UAS), co-immunoprecipitation of CycB-Emb-Nup62 complex, rescue experiments with CycB/active CDK1 overexpression, fluorescence imaging\",\n      \"journal\": \"Cells\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Co-IP of ternary complex, genetic KD with rescue, Drosophila model, single lab\",\n      \"pmids\": [\"31979075\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Nup62 associates with mitotic spindle microtubules (not spindle matrix); its spindle localization depends on its three coiled-coil domains, not on CRM1 (though Nup62 interacts with CRM1 during mitosis). Nup62 knockdown causes defects in chromosome alignment and spindle assembly, with polar chromosome congression defects in >30% of depleted cells.\",\n      \"method\": \"RNAi knockdown, immunofluorescence, domain deletion analysis, spindle association fractionation\",\n      \"journal\": \"Cell biology international\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 / Moderate — KD with defined mitotic phenotype, domain mapping for spindle localization, single lab\",\n      \"pmids\": [\"27298184\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"Nuclear import of HPV16 E7 oncoprotein is mediated via hydrophobic interactions between a patch of residues (65LRLCV69) in the E7 zinc-binding domain and the FG domain of Nup62; an intact zinc-binding domain and specific cysteine residues are required for this importin-independent nuclear import pathway.\",\n      \"method\": \"Mutagenesis of cysteine and hydrophobic residues, EGFP-fusion nuclear localization assays, functional import analysis\",\n      \"journal\": \"Virology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 / Moderate — mutagenesis with nuclear localization readout, single lab, mechanism inferred from localization changes\",\n      \"pmids\": [\"24074597\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"NUP62 overexpression stabilizes NUP88 by inhibiting proteasome-mediated degradation of Nup88; the Nup88-Nup62 interaction is independent of Nup glycosylation status and cell-cycle stage. Stabilized Nup88 interacts with NF-κB (p65) and partially sequesters it into the nucleus of unstimulated cells, inducing NF-κB target genes (Akt, c-myc, IL-6, BIRC3).\",\n      \"method\": \"Co-immunoprecipitation, proteasome inhibitor experiments, siRNA knockdown, NF-κB target gene expression analysis, patient sample validation\",\n      \"journal\": \"Frontiers in oncology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 / Moderate — Co-IP, proteasome inhibition showing Nup62-dependent Nup88 stability, functional NF-κB pathway output, single lab\",\n      \"pmids\": [\"36845732\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"The structured C-terminal coiled-coil domain of Nup62 (not its N-terminal FG-repeat domain) is the dominant determinant for binding FUS and inducing co-phase separation of FUS/Nup62 into amorphous assemblies; expression of isolated C-terminal domain in human cells is sufficient for nuclear envelope localization.\",\n      \"method\": \"In vitro phase separation assay with recombinant proteins, domain deletion analysis, biochemical binding assays, fluorescence microscopy in human cells\",\n      \"journal\": \"Journal of molecular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reconstituted in vitro with recombinant proteins, domain mapping, cellular localization validation, single lab\",\n      \"pmids\": [\"36690069\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"NUP62 promotes nuclear transport of the transcription factor E2F1, which in turn stimulates transcription of the epigenetic enzyme NSD2; NSD2-dependent H3K36me2/H3K36me3 modifications of anti-aging genes (HMGA1, HMGA2, SIRT6) mediate NUP62's role in alleviating senescence in dental pulp stem cells.\",\n      \"method\": \"RNA-seq, epigenomic landscape analysis, NUP62 overexpression/knockdown, nuclear transport assay for E2F1, in vitro and in vivo differentiation assays\",\n      \"journal\": \"International journal of oral science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 / Moderate — functional KD/OE with pathway placement via E2F1 nuclear transport and NSD2 epigenetics, single lab\",\n      \"pmids\": [\"40246825\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"NUP62 competitively binds KEAP1, preventing KEAP1-mediated ubiquitination and degradation of NRF2; this stabilizes NRF2 and promotes its nuclear translocation, enhancing transcription of antioxidant genes and inhibiting ferroptosis in breast cancer cells.\",\n      \"method\": \"Co-immunoprecipitation, ubiquitination assay, NRF2 stability/nuclear localization assay, siRNA knockdown, xenograft in vivo model\",\n      \"journal\": \"iScience\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 / Moderate — Co-IP, ubiquitination assay, functional NRF2 localization and target gene readout, single lab\",\n      \"pmids\": [\"42016308\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"NUP62 knockdown reduces survivin protein levels through the ubiquitin-proteasome system (enhanced ubiquitination and shortened protein half-life); survivin downregulation mediates NUP62-knockdown-induced apoptosis via caspase-3 activation in osimertinib-resistant NSCLC cells.\",\n      \"method\": \"siRNA knockdown, ubiquitination assay, cycloheximide chase (protein half-life), caspase-3 activity assay, survivin overexpression rescue, xenograft in vivo\",\n      \"journal\": \"British journal of cancer\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 / Moderate — ubiquitination assay, protein stability measurement, rescue experiment, single lab\",\n      \"pmids\": [\"42185638\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"NUP62 and NUP214 are differentially distributed between nuclear pore complexes on flattened nuclear surfaces and the peripheral rim, indicating architectural heterogeneity among NPC populations in adherent cells.\",\n      \"method\": \"STED super-resolution immunofluorescence microscopy, orthogonal imaging of cell nuclei\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single imaging-based localization study, no functional consequence tested, single lab\",\n      \"pmids\": [\"22558357\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"Reduction of Nup62 content enhances density-induced myoblast differentiation in high-mitogen medium, while forced Nup62 expression inhibits density-induced differentiation; this effect involves p38 MAP kinase activation. Differentiation induced by low-mitogen medium is unaffected by ectopic Nup62 expression.\",\n      \"method\": \"siRNA knockdown, ectopic overexpression, differentiation assay, p38 MAP kinase activation readout in C2C12 myoblasts\",\n      \"journal\": \"Differentiation; research in biological diversity\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — KD/OE with differentiation phenotype, p38 pathway involvement shown but mechanism not fully characterized, single lab\",\n      \"pmids\": [\"32554220\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"During post-mitotic NPC assembly, degrading Nup62 arrests assembly at an intermediate step with smaller membrane pores and removes the whole central transport channel; 32 copies of the central channel subcomplex self-associate via hydrophobic interactions to occupy the pore center and exert an outward pushing force for full pore dilation. Disrupting these hydrophobic interactions during assembly blocked pore dilation, impaired nuclear import, and caused smaller nuclei and looser NE spacing.\",\n      \"method\": \"Acute molecular perturbations in live cells combined with correlative 3D electron tomography and MINFLUX super-resolution microscopy, molecular dynamics simulations\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — structural imaging (ET + MINFLUX), live-cell perturbation, MD simulations; preprint not yet peer-reviewed\",\n      \"pmids\": [],\n      \"is_preprint\": true\n    }\n  ],\n  \"current_model\": \"NUP62 is a central channel nucleoporin that forms a dynamic heterocomplex with Nup54 and Nup58 (via coiled-coil interactions) to build the NPC transport channel, directly mediates nuclear import of diverse cargos (including MUC1-C, GR-hsp90, β-catenin, ΔNp63α, and viral proteins) through FG-repeat and coiled-coil domain interactions, undergoes regulatory post-translational modifications (TIP60-mediated acetylation at K432 during mitosis to remodel the Nup62 complex and direct spindle orientation; PYK2-mediated phosphorylation at Y422 to release it from the NPC), and has non-canonical roles at the mitotic spindle (chromosome alignment, SAC maintenance), at the leading edge of migrating cells (via Exo70 interaction), and in pathological contexts including ALS/FTLD (cytoplasmic mislocalization promotes TDP-43 insolubility) and viral infection (2A protease cleavage of FG-repeat domain disrupts nucleocytoplasmic transport).\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"NUP62 is a central-channel nucleoporin that builds the transport conduit of the nuclear pore complex and serves as a hub for both classical and importin-independent nuclear translocation of diverse cargos [#5, #12]. Structurally, it forms a dynamic triple complex with Nup54 and Nup58 in which Nup54 bridges the two partners through its ordered \\u03b1-helical regions, assembling at a 4:2:1 stoichiometry; its C-terminal segment adopts a parallel three-helix coiled-coil bundle [#12, #13]. During post-mitotic NPC assembly, self-association of many copies of this central-channel subcomplex via hydrophobic interactions occupies and dilates the pore, and loss of NUP62 arrests assembly with smaller pores and impaired import [#26]. The protein engages cargo through two functionally distinct modules: its FG-repeat region binds substrates such as \\u03b2-catenin, \\u0394Np63\\u03b1, and viral oncoproteins (HPV16 E7), while its structured coiled-coil domain mediates partner interactions including Exo70 and FUS [#5, #4, #18, #11, #20]. NUP62 thereby controls nuclear import of multiple signaling and oncogenic factors\\u2014the MUC1-C oncoprotein, the GR-hsp90 chaperone heterocomplex, \\u03b2-catenin, and \\u0394Np63\\u03b1 [#0, #1, #5, #4]. Beyond the pore, NUP62 has non-canonical roles: TIP60-mediated acetylation at Lys432 dissolves the Nup62\\u2013Nup58\\u2013Nup54 complex at mitotic entry and redirects NUP62 to the mitotic spindle to control spindle orientation and chromosome segregation, and NUP62 is independently required for centrosome integrity, spindle-assembly-checkpoint function, and chromosome alignment [#14, #7, #15, #17]. At the leading edge of migrating cells it is recruited to the plasma membrane by Exo70 via its coiled-coil domain to promote migration [#11]. A recessive Q391P missense mutation in NUP62 causes infantile bilateral striatal necrosis, and the same residue is critical for spindle-checkpoint function [#2, #15]. In ALS/FTLD, NUP62 mislocalizes to the cytoplasm where it binds TDP-43 and promotes its insolubility and inclusion formation [#9]. NUP62 activity is regulated by post-translational modification, including ROCK and PYK2 phosphorylation of its FG/Y422 regions, the latter releasing it from the pore [#4, #10].\",\n  \"teleology\": [\n    {\n      \"year\": 2006,\n      \"claim\": \"Established that NUP62 has a non-redundant, cell-type-specific physiological requirement, linking this nucleoporin to a defined human disease.\",\n      \"evidence\": \"Genetic mapping and Sanger sequencing of a Q391P missense mutation co-segregating across 8 families with infantile bilateral striatal necrosis\",\n      \"pmids\": [\"16786527\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not explain why basal ganglia neurons are selectively vulnerable\", \"Molecular consequence of Q391P on NPC function not resolved here\"]\n    },\n    {\n      \"year\": 2007,\n      \"claim\": \"Showed NUP62 acts as a direct import receptor for an oncogenic cargo, defining a binding mechanism dependent on cargo oligomerization.\",\n      \"evidence\": \"Co-IP, direct binding with purified components, and CQC-motif mutagenesis abolishing MUC1-C oligomerization, Nup62 binding, and nuclear localization\",\n      \"pmids\": [\"17500061\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether import is importin-independent not established\", \"Did not map the precise FG vs coiled-coil contribution to cargo affinity\"]\n    },\n    {\n      \"year\": 2009,\n      \"claim\": \"Extended the cargo repertoire to a chaperoned receptor complex and to the actin-cytoskeleton/migration machinery, revealing NUP62 functions beyond the central channel.\",\n      \"evidence\": \"Digitonin-permeabilized transport assays with the GR-hsp90 heterocomplex; direct binding and domain-deletion mapping of Exo70 to the coiled-coil domain with migration knockdown\",\n      \"pmids\": [\"19581287\", \"19552648\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Stoichiometry of GR-hsp90 docking on NUP62 not defined\", \"How the same coiled-coil serves both NPC assembly and leading-edge recruitment unclear\"]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Demonstrated that pathogens disable nucleocytoplasmic transport by directly proteolyzing NUP62, defining its FG region as a viral target.\",\n      \"evidence\": \"In vitro cleavage of bacterially expressed Nup62 by purified rhinovirus 2A protease, cleavage-site mutagenesis, and domain-specific antibodies in infected cells\",\n      \"pmids\": [\"20622012\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Quantitative contribution of NUP62 cleavage versus other nucleoporins to transport collapse not isolated\"]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Resolved cargo-specific binding determinants, showing the FG repeats engage \\u03b2-catenin Arm repeats and that NUP62 rate-limits its bidirectional transport.\",\n      \"evidence\": \"FRAP in live cells, in vitro binding with purified components mapping Arm repeats R3-8/R10-12, and siRNA knockdown comparison with importin-\\u03b2; separate Y2H/BiFC/Co-IP placing NUP62 downstream of ORP8 in SREBP regulation\",\n      \"pmids\": [\"22110128\", \"21698267\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"ORP8 epistasis is Medium-confidence and lacks reconstitution\", \"Whether \\u03b2-catenin transport is fully importin-independent not settled\"]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Uncovered a non-canonical mitotic role at centrosomes and added a viral cargo using importin-independent FG binding.\",\n      \"evidence\": \"RNAi depletion producing centrosome segregation, centriole maturation, and spindle-orientation defects; mutagenesis mapping HPV16 E7 zinc-binding-domain residues to the FG domain\",\n      \"pmids\": [\"24107630\", \"24074597\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Centrosome phenotype could be indirect via global transport defects\", \"E7 import mechanism inferred from localization, not direct flux measurement\"]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Identified ICP27 as a viral inhibitor that hijacks NUP62 binding to block both importin and transportin pathways.\",\n      \"evidence\": \"Co-IP and in vitro binding with purified components, point mutagenesis of ICP27, and import inhibition assays\",\n      \"pmids\": [\"22334672\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Mechanism by which ICP27-NUP62 binding blocks multiple receptor pathways not defined\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Defined phosphoregulation that releases NUP62 from the pore and linked it to neuronal architecture.\",\n      \"evidence\": \"PYK2 phosphorylation at Y422/Y425 with fractionation showing NPC shedding; RNAi in primary neurons causing dendritic retraction; in vivo stressed hippocampus\",\n      \"pmids\": [\"25349423\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Causal link between Y422 phosphorylation and dendritic phenotype not directly tested\", \"Single lab\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Provided the structural basis for the central-channel heterocomplex, defining Nup54 as the bridging subunit and the 4:2:1 stoichiometry.\",\n      \"evidence\": \"Crystal structures plus solution biophysics (SEC, SEC-MALS) of the Nup62-Nup54-Nup58 ordered regions\",\n      \"pmids\": [\"26025361\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not show how the assembled complex behaves within an intact pore\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Localized NUP62 to spindle microtubules and showed its coiled-coil domains, not FG repeats or CRM1, drive spindle targeting and chromosome alignment.\",\n      \"evidence\": \"RNAi knockdown, immunofluorescence, domain-deletion analysis, and spindle fractionation\",\n      \"pmids\": [\"27298184\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct microtubule-binding partner on the spindle not identified\", \"Single lab\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Solved the coiled-coil structure and demonstrated a chain-replacement mechanism enabling NUP62 to switch between NPC and non-NPC partners; ROCK phosphorylation tunes \\u0394Np63\\u03b1 import in cancer.\",\n      \"evidence\": \"2.4 \\u00c5 crystal structure, SEC-MALS, cross-linking, and in vitro Exo70 binding; siRNA/Co-IP/phosphorylation and proliferation-differentiation assays in SCC\",\n      \"pmids\": [\"28406021\", \"29217659\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"In vivo relevance of homo- versus hetero-oligomer switching not established\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Connected NUP62 to spindle-assembly-checkpoint fidelity and meiotic cell-cycle progression, with the disease residue Q391 implicated in checkpoint function.\",\n      \"evidence\": \"siRNA knockdown and Q391P overexpression with SAC and aneuploidy readouts; Drosophila Co-IP of a CycB-Emb-Nup62 export complex with knockdown and rescue\",\n      \"pmids\": [\"32905854\", \"31979075\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism linking Q391 to SAC not resolved\", \"CycB export role demonstrated in Drosophila, human conservation untested\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Defined acetylation as a mitotic switch remodeling the NUP62 complex and revealed a pathological cytoplasmic gain-of-function in neurodegeneration.\",\n      \"evidence\": \"In vitro TIP60 acetylation, K432 acetyl-mimetic/defective mutants with spindle/segregation readouts; iPSC neuron models, Co-IP/fractionation, and postmortem ALS/FTLD tissue showing NUP62:TDP-43 inclusions\",\n      \"pmids\": [\"36190325\", \"35697676\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"How K432 acetylation directs spindle targeting mechanistically unclear\", \"Whether NUP62 mislocalization is cause or consequence of TDP-43 pathology not resolved\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Established that the structured C-terminal domain, not the FG region, drives phase separation with FUS and that NUP62 stabilizes other nucleoporins to influence signaling output.\",\n      \"evidence\": \"In vitro phase separation with recombinant FUS/Nup62 and domain mapping; Co-IP and proteasome-inhibition experiments showing Nup62-dependent Nup88 stabilization and NF-\\u03baB activation\",\n      \"pmids\": [\"36690069\", \"36845732\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Physiological role of FUS/NUP62 co-phase separation not defined\", \"Nup88/NF-\\u03baB axis from single lab\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Placed NUP62 upstream of transcriptional and epigenetic programs governing senescence and antioxidant defense via cargo-specific transport.\",\n      \"evidence\": \"RNA-seq/epigenomics with NUP62 OE/KD and E2F1 nuclear-transport assays linking to NSD2 anti-aging genes; Co-IP/ubiquitination assays placing NUP62 as a KEAP1 competitor stabilizing NRF2\",\n      \"pmids\": [\"40246825\", \"42016308\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether E2F1 and NRF2 effects are direct transport functions or indirect not fully separated\", \"Single lab per pathway\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Linked NUP62 to apoptotic control in drug-resistant cancer through proteostatic regulation of survivin.\",\n      \"evidence\": \"siRNA knockdown, ubiquitination assay, cycloheximide chase, caspase-3 assay, survivin rescue, and xenograft in osimertinib-resistant NSCLC\",\n      \"pmids\": [\"42185638\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct versus indirect mechanism by which NUP62 controls survivin stability unclear\", \"Single context (resistant NSCLC)\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How NUP62's mitotic, leading-edge, transcriptional, and proteostatic functions are coordinated with its core channel role, and which functions are direct versus secondary to global transport changes, remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No unified model distinguishing on-pore from off-pore activities\", \"Most non-canonical roles rest on single-lab studies\", \"In vivo significance of post-translational switches beyond mitosis unknown\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140104\", \"supporting_discovery_ids\": [0, 1, 5, 4, 18]},\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [12, 13, 26]},\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [17]},\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [19, 22, 23]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005635\", \"supporting_discovery_ids\": [12, 24, 6, 20]},\n      {\"term_id\": \"GO:0005815\", \"supporting_discovery_ids\": [7]},\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [17, 14]},\n      {\"term_id\": \"GO:0005886\", \"supporting_discovery_ids\": [11]},\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [9, 10]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-9609507\", \"supporting_discovery_ids\": [0, 1, 5, 12, 26]},\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [7, 14, 15, 17]},\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [4, 19, 22]},\n      {\"term_id\": \"R-HSA-1643685\", \"supporting_discovery_ids\": [2, 9]}\n    ],\n    \"complexes\": [\n      \"Nup62-Nup54-Nup58 central channel subcomplex\",\n      \"nuclear pore complex\"\n    ],\n    \"partners\": [\n      \"NUP54\",\n      \"NUP58\",\n      \"EXOC7\",\n      \"FUS\",\n      \"NUP88\",\n      \"CTNNB1\",\n      \"KEAP1\",\n      \"TARDBP\"\n    ],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":9,"faith_total":9,"faith_pct":100.0}}