Affinage

NUP62

Nuclear pore glycoprotein p62 · UniProt P37198

Length
522 aa
Mass
53.3 kDa
Annotated
2026-06-10
37 papers in source corpus 26 papers cited in narrative 27 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 9/9 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

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).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 2006 High

    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

    PMID:16786527

    Open questions at the time
    • Does not explain why basal ganglia neurons are selectively vulnerable
    • Molecular consequence of Q391P on NPC function not resolved here
  2. 2007 High

    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

    PMID:17500061

    Open questions at the time
    • Whether import is importin-independent not established
    • Did not map the precise FG vs coiled-coil contribution to cargo affinity
  3. 2009 High

    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

    PMID:19552648 PMID:19581287

    Open questions at the time
    • Stoichiometry of GR-hsp90 docking on NUP62 not defined
    • How the same coiled-coil serves both NPC assembly and leading-edge recruitment unclear
  4. 2010 High

    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

    PMID:20622012

    Open questions at the time
    • Quantitative contribution of NUP62 cleavage versus other nucleoporins to transport collapse not isolated
  5. 2011 High

    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

    PMID:21698267 PMID:22110128

    Open questions at the time
    • ORP8 epistasis is Medium-confidence and lacks reconstitution
    • Whether β-catenin transport is fully importin-independent not settled
  6. 2013 Medium

    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

    PMID:24074597 PMID:24107630

    Open questions at the time
    • Centrosome phenotype could be indirect via global transport defects
    • E7 import mechanism inferred from localization, not direct flux measurement
  7. 2012 High

    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

    PMID:22334672

    Open questions at the time
    • Mechanism by which ICP27-NUP62 binding blocks multiple receptor pathways not defined
  8. 2014 Medium

    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

    PMID:25349423

    Open questions at the time
    • Causal link between Y422 phosphorylation and dendritic phenotype not directly tested
    • Single lab
  9. 2015 High

    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

    PMID:26025361

    Open questions at the time
    • Does not show how the assembled complex behaves within an intact pore
  10. 2016 Medium

    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

    PMID:27298184

    Open questions at the time
    • Direct microtubule-binding partner on the spindle not identified
    • Single lab
  11. 2017 High

    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

    PMID:28406021 PMID:29217659

    Open questions at the time
    • In vivo relevance of homo- versus hetero-oligomer switching not established
  12. 2020 Medium

    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

    PMID:31979075 PMID:32905854

    Open questions at the time
    • Mechanism linking Q391 to SAC not resolved
    • CycB export role demonstrated in Drosophila, human conservation untested
  13. 2022 High

    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

    PMID:35697676 PMID:36190325

    Open questions at the time
    • How K432 acetylation directs spindle targeting mechanistically unclear
    • Whether NUP62 mislocalization is cause or consequence of TDP-43 pathology not resolved
  14. 2023 Medium

    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

    PMID:36690069 PMID:36845732

    Open questions at the time
    • Physiological role of FUS/NUP62 co-phase separation not defined
    • Nup88/NF-κB axis from single lab
  15. 2025 Medium

    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

    PMID:40246825 PMID:42016308

    Open questions at the time
    • Whether E2F1 and NRF2 effects are direct transport functions or indirect not fully separated
    • Single lab per pathway
  16. 2026 Medium

    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

    PMID:42185638

    Open questions at the time
    • Direct versus indirect mechanism by which NUP62 controls survivin stability unclear
    • Single context (resistant NSCLC)

Open questions

Synthesis pass · forward-looking unresolved questions
  • 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.
  • 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

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140104 molecular carrier activity 5 GO:0005198 structural molecule activity 3 GO:0098772 molecular function regulator activity 3 GO:0008092 cytoskeletal protein binding 1
Localization
GO:0005635 nuclear envelope 4 GO:0005829 cytosol 2 GO:0005856 cytoskeleton 2 GO:0005815 microtubule organizing center 1 GO:0005886 plasma membrane 1
Pathway
R-HSA-9609507 Protein localization 5 R-HSA-1640170 Cell Cycle 4 R-HSA-162582 Signal Transduction 3 R-HSA-1643685 Disease 2
Partners
CTNNB1EXOC7FUSKEAP1NUP54NUP58NUP88TARDBP
Complex memberships
Nup62-Nup54-Nup58 central channel subcomplexnuclear pore complex

Evidence

Reading pass · 27 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2007 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. Co-immunoprecipitation, direct binding assays with purified components, site-directed mutagenesis, stable expression of mutant constructs with nuclear localization readout The Journal of biological chemistry High 17500061
2009 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. Co-immunoprecipitation, radicicol hsp90 inhibition, TPR peptide competition, digitonin-permeabilized cell nuclear transport assay Molecular and cellular biology High 19581287
2006 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. Genetic mapping, Sanger sequencing of candidate region, mutation co-segregation analysis across 8 families Annals of neurology High 16786527
2010 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. 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 The Journal of biological chemistry High 20622012
2017 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. siRNA knockdown, co-immunoprecipitation, phosphorylation assays, nuclear transport assays, differentiation/proliferation assays EMBO reports High 29217659
2011 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. FRAP in live cells, in vitro binding assay with purified components (direct interaction), siRNA knockdown, proteomics screen The Journal of biological chemistry High 22110128
2011 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. Yeast two-hybrid, bimolecular fluorescence complementation (BiFC), co-immunoprecipitation, confocal immunofluorescence, siRNA knockdown epistasis PloS one Medium 21698267
2013 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. RNAi knockdown, immunofluorescence microscopy, cell cycle analysis Cell cycle (Georgetown, Tex.) Medium 24107630
2012 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. Co-immunoprecipitation, in vitro binding with purified components, deletion and point mutagenesis, nuclear import assays The Journal of biological chemistry High 22334672
2022 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. iPSC neuron models, co-immunoprecipitation/co-localization, solubility fractionation, postmortem tissue immunostaining Nature communications High 35697676
2014 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. Phosphorylation assay in cultured cells, fractionation, immunofluorescence in chronically stressed rat hippocampus, RNAi knockdown in primary neurons with morphological readout Proceedings of the National Academy of Sciences of the United States of America Medium 25349423
2009 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. Direct binding assay, co-immunoprecipitation, confocal microscopy, siRNA knockdown, cell migration assay Traffic (Copenhagen, Denmark) High 19552648
2015 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. Size exclusion chromatography, solution biophysics (SEC-MALS, analytical ultracentrifugation implied), crystal structure analysis The Journal of biological chemistry High 26025361
2017 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. X-ray crystallography (2.4 Å), SEC-MALS, glutaraldehyde cross-linking, in vitro binding assay Biochemistry High 28406021
2022 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. In vitro acetylation assay, mutagenesis (acetylation-mimetic/defective mutants), immunofluorescence, siRNA knockdown with spindle/chromosome segregation readouts Journal of molecular cell biology High 36190325
2020 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. siRNA knockdown, overexpression of Q391P mutant, mitotic timing analysis, immunofluorescence for SAC components, aneuploidy assay in neural stem cells The international journal of biochemistry & cell biology Medium 32905854
2020 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. dsRNA-mediated knockdown (Gal4/UAS), co-immunoprecipitation of CycB-Emb-Nup62 complex, rescue experiments with CycB/active CDK1 overexpression, fluorescence imaging Cells Medium 31979075
2016 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. RNAi knockdown, immunofluorescence, domain deletion analysis, spindle association fractionation Cell biology international Medium 27298184
2013 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. Mutagenesis of cysteine and hydrophobic residues, EGFP-fusion nuclear localization assays, functional import analysis Virology Medium 24074597
2023 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). Co-immunoprecipitation, proteasome inhibitor experiments, siRNA knockdown, NF-κB target gene expression analysis, patient sample validation Frontiers in oncology Medium 36845732
2023 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. In vitro phase separation assay with recombinant proteins, domain deletion analysis, biochemical binding assays, fluorescence microscopy in human cells Journal of molecular biology Medium 36690069
2025 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. RNA-seq, epigenomic landscape analysis, NUP62 overexpression/knockdown, nuclear transport assay for E2F1, in vitro and in vivo differentiation assays International journal of oral science Medium 40246825
2026 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. Co-immunoprecipitation, ubiquitination assay, NRF2 stability/nuclear localization assay, siRNA knockdown, xenograft in vivo model iScience Medium 42016308
2026 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. siRNA knockdown, ubiquitination assay, cycloheximide chase (protein half-life), caspase-3 activity assay, survivin overexpression rescue, xenograft in vivo British journal of cancer Medium 42185638
2012 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. STED super-resolution immunofluorescence microscopy, orthogonal imaging of cell nuclei PloS one Low 22558357
2020 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. siRNA knockdown, ectopic overexpression, differentiation assay, p38 MAP kinase activation readout in C2C12 myoblasts Differentiation; research in biological diversity Low 32554220
2025 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. Acute molecular perturbations in live cells combined with correlative 3D electron tomography and MINFLUX super-resolution microscopy, molecular dynamics simulations bioRxivpreprint Medium

Source papers

Stage 0 corpus · 37 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2007 Nuclear import of the MUC1-C oncoprotein is mediated by nucleoporin Nup62. The Journal of biological chemistry 130 17500061
2009 Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin beta. Molecular and cellular biology 119 19581287
2006 Mutated nup62 causes autosomal recessive infantile bilateral striatal necrosis. Annals of neurology 105 16786527
2010 Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease. The Journal of biological chemistry 83 20622012
2017 ROCK-dependent phosphorylation of NUP62 regulates p63 nuclear transport and squamous cell carcinoma proliferation. EMBO reports 67 29217659
2011 Specific armadillo repeat sequences facilitate β-catenin nuclear transport in live cells via direct binding to nucleoporins Nup62, Nup153, and RanBP2/Nup358. The Journal of biological chemistry 65 22110128
2011 OSBP-related protein 8 (ORP8) regulates plasma and liver tissue lipid levels and interacts with the nucleoporin Nup62. PloS one 53 21698267
2013 Nucleoporin Nup62 maintains centrosome homeostasis. Cell cycle (Georgetown, Tex.) 49 24107630
2012 Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathways. The Journal of biological chemistry 44 22334672
2022 NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility. Nature communications 43 35697676
2014 Role for NUP62 depletion and PYK2 redistribution in dendritic retraction resulting from chronic stress. Proceedings of the National Academy of Sciences of the United States of America 36 25349423
2009 Exo70-mediated recruitment of nucleoporin Nup62 at the leading edge of migrating cells is required for cell migration. Traffic (Copenhagen, Denmark) 29 19552648
2025 Exploring NUP62's role in cancer progression, tumor immunity, and treatment response: insights from multi-omics analysis. Frontiers in immunology 24 40098960
2005 Alternative pre-mRNA processing regulates cell-type specific expression of the IL4l1 and NUP62 genes. BMC biology 23 16029492
2012 Nuclear distributions of NUP62 and NUP214 suggest architectural diversity and spatial patterning among nuclear pore complexes. PloS one 19 22558357
2023 Overexpressed Nup88 stabilized through interaction with Nup62 promotes NF-κB dependent pathways in cancer. Frontiers in oncology 17 36845732
2015 Ordered Regions of Channel Nucleoporins Nup62, Nup54, and Nup58 Form Dynamic Complexes in Solution. The Journal of biological chemistry 15 26025361
2017 Nup62-mediated nuclear import of p63 in squamous cell carcinoma. EMBO reports 14 29254932
2020 Nuclear Export of Cyclin B Mediated by the Nup62 Complex Is Required for Meiotic Initiation in Drosophila Males. Cells 12 31979075
2017 The Nup62 Coiled-Coil Motif Provides Plasticity for Triple-Helix Bundle Formation. Biochemistry 11 28406021
2006 Functional analysis of nuclear pore complex protein Nup62/p62 using monoclonal antibodies. Hybridoma (2005) 11 16704304
2022 Acetylation of Nup62 by TIP60 ensures accurate chromosome segregation in mitosis. Journal of molecular cell biology 10 36190325
2020 NUP62 is required for the maintenance of the spindle assembly checkpoint and chromosomal stability. The international journal of biochemistry & cell biology 9 32905854
2023 Regulation of FLC nuclear import by coordinated action of the NUP62-subcomplex and importin β SAD2. Journal of integrative plant biology 8 37278318
2016 Nup62, associated with spindle microtubule rather than spindle matrix, is involved in chromosome alignment and spindle assembly during mitosis. Cell biology international 8 27298184
2013 Nuclear import of high risk HPV16 E7 oncoprotein is mediated by its zinc-binding domain via hydrophobic interactions with Nup62. Virology 8 24074597
2025 NUP62 alleviates senescence and promotes the stemness of human dental pulp stem cells via NSD2-dependent epigenetic reprogramming. International journal of oral science 6 40246825
2023 Interactions between FUS and the C-terminal Domain of Nup62 are Sufficient for their Co-phase Separation into Amorphous Assemblies. Journal of molecular biology 6 36690069
2023 RNA-seq reveals Nup62 as a potential regulator for cell division after traumatic brain injury in mice hippocampus. PeerJ 6 36908815
2022 Mislocalization of Nup62 Contributes to TDP-43 Proteinopathy in ALS/FTLD. ACS chemical neuroscience 6 36001801
2023 Cyclin B Export to the Cytoplasm via the Nup62 Subcomplex and Subsequent Rapid Nuclear Import Are Required for the Initiation of Drosophila Male Meiosis. Cells 4 37998346
2019 NUP62: the target of an anti-sperm auto-monoclonal antibody during testicular development. Reproduction (Cambridge, England) 4 31585439
2013 [The 2A protease of enterovirus 71 cleaves nup62 to inhibit nuclear transport]. Bing du xue bao = Chinese journal of virology 4 23895008
2026 NUP62 Elevates USP10 Expression and Promotes Tamoxifen Resistance of Breast Cancer by Deubiquitinating ERα. Annals of surgical oncology 1 41501594
2026 NUP62 promotes breast cancer progression and inhibits ferroptosis by stabilizing NRF2 in a KEAP1-dependent way. iScience 0 42016308
2026 Silencing of NUP62 overcomes osimertinib resistance via ubiquitination of survivin in non-small cell lung cancer cells. British journal of cancer 0 42185638
2020 Changes in Nup62 content affect contact-induced differentiation of cultured myoblasts. Differentiation; research in biological diversity 0 32554220

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