Affinage

NUP153

Nuclear pore complex protein Nup153 · UniProt P49790

Length
1475 aa
Mass
153.9 kDa
Annotated
2026-04-29
66 papers in source corpus 46 papers cited in narrative 46 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NUP153 is a dynamic FG-repeat nucleoporin of the nuclear basket that serves as a central scaffold for nucleocytoplasmic transport, NPC assembly, chromatin regulation, and mitotic checkpoint control. Its C-terminal XFXFG-repeat domain provides direct docking sites for importin α/β and transportin to mediate classical NLS and M9-dependent nuclear import, and is required for mRNA, snRNA, and rRNA export; the same FG repeats and an adjacent RRR motif engage HIV-1 capsid lattices at hexamer and tri-hexamer interfaces to enable viral preintegration complex nuclear entry in non-dividing cells (PMID:9531546, PMID:9889100, PMID:10069809, PMID:24130490, PMID:36943880). The N-terminal domain anchors NUP153 at the inner nuclear membrane via an amphipathic helix required for interphasic NPC assembly and recruitment of the Nup107-160 complex, scaffolds Tpr, Nup50, SENP1/SENP2, and Mad1 at the basket, and interacts with A- and B-type lamins to couple NPC positioning to nuclear architecture (PMID:26051542, PMID:12802065, PMID:22688647, PMID:21327106, PMID:21983083). Beyond transport, NUP153 binds chromatin at developmental gene promoters to recruit PRC1 for epigenetic silencing in embryonic stem cells, cooperates with Sox2 to regulate neural progenitor gene expression, localizes SENP1 to NPCs to control 53BP1 sumoylation and NHEJ pathway choice, and is itself targeted for proteasomal degradation by the Cul3–SPOP E3 ligase (PMID:26080816, PMID:28919367, PMID:28576968, PMID:39785820).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 1994 Medium

    Cloning of human NUP153 defined the domain architecture—33 XFXFG repeats, four zinc fingers, and O-GlcNAc modification—establishing the molecular framework for all subsequent functional dissection.

    Evidence cDNA sequencing and domain prediction

    PMID:8110839

    Open questions at the time
    • No functional data for individual domains
    • Zinc finger ligands unknown
    • Post-translational modification roles untested
  2. 1998 High

    Systematic domain mapping revealed that the N-terminal domain targets NUP153 to the NPC and nuclear envelope, while the C-terminal FG domain serves as a direct binding platform for importin β and transportin, with separate sites mediating the classical NLS and M9 import pathways.

    Evidence Deletion-reporter fusions in cells; in vitro binding with purified importin β and dominant-negative fragment import assays in Xenopus

    PMID:9531546 PMID:9745047 PMID:9889100

    Open questions at the time
    • How NUP153 coordinates simultaneous binding of multiple import receptors in vivo
    • Structural basis of pathway-specific binding sites unresolved
  3. 1999 High

    Discovery that NUP153 contains a zinc-finger Ran-binding domain and an M9 NLS for transportin, and that RanGTP differentially regulates import vs. export receptor interactions, established NUP153 as a Ran-regulated, bidirectional transport platform; simultaneously, antibody-blocking experiments showed NUP153 is required for export of mRNA, snRNA, rRNA, and NES proteins.

    Evidence Phage display; co-IP; RanGTP-regulated binding assays; antibody microinjection in Xenopus oocytes; RNA export assays

    PMID:10069809 PMID:10202161

    Open questions at the time
    • RNA binding domain not yet mapped
    • Mechanism of NUP153 shuttling between NPC faces unclear
  4. 2000 High

    Reconstitution experiments demonstrated that NUP153 is essential for nuclear basket assembly and NPC anchoring; NPCs assembled without NUP153 lack basket components, are mobile in the envelope, and are selectively deficient in importin α/β-mediated import; NUP153 incorporation itself requires prior lamin assembly, linking it to the lamina.

    Evidence Immunodepletion from Xenopus egg extracts; immunogold EM; co-IP showing lamin B3 binding; nuclear transport assays

    PMID:10921874 PMID:11598013

    Open questions at the time
    • Which lamin interaction domain is critical for NPC anchoring
    • Whether lamin dependency applies in somatic cells
  5. 2001 High

    Identification of a conserved RNA-binding domain (aa 250–400) revealed that NUP153 directly engages RNA substrates, with subsequent studies showing loose sequence selectivity favoring single-stranded mRNA over structured RNAs.

    Evidence In vitro RNA binding with recombinant fragments; cross-species comparison; systematic RNA substrate panel

    PMID:11567018 PMID:14681581 PMID:17242408

    Open questions at the time
    • In vivo RNA targets not identified
    • Functional consequence of RNA binding on specific transcript export unclear
  6. 2003 High

    NUP153 was shown to scaffold Tpr and Nup50 at the nuclear basket (their localization depends on NUP153), and to recruit the COPI coatomer complex via its zinc finger domain to direct nuclear envelope breakdown at mitosis.

    Evidence RNAi; affinity chromatography; yeast two-hybrid; Xenopus NE breakdown assay with immunodepletion and rescue

    PMID:12802065 PMID:12967567

    Open questions at the time
    • Whether Tpr contributes reciprocally to NUP153 stability
    • COPI-mediated vesiculation mechanism not fully resolved
  7. 2004 High

    FRAP studies established that NUP153 is a constitutively mobile nucleoporin whose exchange on/off the NPC depends on active RNA Pol I/II transcription, distinguishing it from stable scaffold nucleoporins and linking it to ongoing gene expression.

    Evidence FRAP of GFP-NUP153 in live HeLa cells with transcription inhibitors; domain deletion analysis

    PMID:14718558

    Open questions at the time
    • Molecular signal coupling transcription to NUP153 mobility unknown
    • Whether RNA binding domain mediates transcription-coupled exchange
  8. 2009 High

    The FG-repeat C-terminal domain was identified as a direct binding partner for HIV-1 integrase and capsid, establishing NUP153 as a host factor for HIV-1 nuclear entry; capsid mutant analysis showed that this dependency is CA-determined and linked to the nuclear import step of the preintegration complex.

    Evidence Semi-permeabilized cell import assays; direct binding with purified proteins; CA mutant panel; qPCR for viral intermediates

    PMID:19369352 PMID:21593146

    Open questions at the time
    • Structural basis of NUP153–CA interaction not yet resolved
    • Whether NUP153 guides integration site selection
  9. 2010 High

    Genome-wide ChIP in Drosophila revealed NUP153 binds large chromatin domains enriched for active transcription marks and regulates thousands of genes including dosage compensation targets, establishing a transport-independent gene-regulatory role; separately, direct binding to Mad1 linked NUP153 to spindle assembly checkpoint regulation.

    Evidence ChIP-chip; RNAi expression profiling in S2 cells; direct in vitro Mad1–NUP153 binding; RNAi and overexpression phenotypes

    PMID:20174442 PMID:21327106

    Open questions at the time
    • How NUP153 chromatin binding is distinguished from NPC-tethered vs. intranuclear pools
    • Whether Mad1 regulation is conserved across species
  10. 2011 High

    NUP153 was shown to interact with both A- and B-type lamins through N- and C-terminal domains, to mediate cargo-specific nuclear import of 53BP1 via importin β, and to facilitate β-catenin NPC traversal through direct FG-repeat engagement, broadening its known transport substrates.

    Evidence GST pull-downs with purified lamins; siRNA screen for 53BP1 import; FRAP and in vitro binding for β-catenin

    PMID:21983083 PMID:22075984 PMID:22110128

    Open questions at the time
    • Structural details of lamin Ig-fold–NUP153 interface lacking
    • Whether 53BP1 import function is separable from 53BP1 DSB recruitment
  11. 2012 High

    Mapping of NUP153–Nup50 and NUP153–SENP1/SENP2 interactions revealed a dual-interface scaffolding system at the basket that controls import efficiency and SUMO protease localization; NUP153 itself is sumoylated and kept in check by basket-localized SENPs.

    Evidence Domain deletion; co-IP; import assays; sumoylation assays; RNAi

    PMID:22688647 PMID:23007389

    Open questions at the time
    • Functional consequence of NUP153 sumoylation on its individual activities unknown
    • Whether SENP2 has transport-independent roles at the basket
  12. 2013 High

    Structural and biochemical dissection showed NUP153 FG motifs bind directly into the CA hexamer α-helix 3/4 hydrophobic pocket (shared with CPSF6 and PF74), with different FG motifs discriminating HIV-1 from EIAV capsids, explaining lentiviral specificity.

    Evidence Trim-NUP153(C) restriction assay; direct binding; CA and NUP153 mutagenesis; competition assays

    PMID:24130490

    Open questions at the time
    • No high-resolution structure of full NUP153(C)–CA complex
    • Whether NUP153 engagement alters CA lattice stability in vivo
  13. 2015 High

    NUP153 was shown to recruit PRC1 to developmental gene promoters in ESCs for epigenetic silencing, and its N-terminal amphipathic helix was found to bind inner nuclear membrane directly to drive interphasic NPC assembly via Nup107-160 complex recruitment, separating its chromatin and structural functions.

    Evidence ChIP-seq; RNAi with PRC1 recruitment assays in mESCs; in vitro membrane binding; domain mutagenesis; live-cell imaging

    PMID:26051542 PMID:26080816

    Open questions at the time
    • How PRC1 recruitment is coordinated with NUP153 mobility
    • Whether amphipathic helix–membrane interaction is regulated by phosphorylation
  14. 2017 High

    NUP153 was placed in the DNA damage repair pathway: it localizes SENP1 to NPCs, which controls 53BP1 sumoylation required for NHEJ; additionally, NUP153/Nup50 promote 53BP1 focus formation at DSBs independently of its import role, antagonizing BRCA1/BARD1 to favor NHEJ over HR; NUP153 also cooperates with Sox2 at chromatin to regulate neural progenitor gene expression.

    Evidence SENP1 artificial tethering rescue; NHEJ reporter assays; epistasis analysis with BRCA1/BARD1; co-IP with Sox2; ChIP-seq and ATAC-seq in neural progenitors

    PMID:28576968 PMID:28751496 PMID:28919367

    Open questions at the time
    • Direct sumoylation sites on 53BP1 regulated by NUP153–SENP1 axis not mapped
    • Whether NUP153–Sox2 function is NPC-tethered or nucleoplasmic
  15. 2018 High

    Crystal structures of HIV-1 CA hexamers with NUP153-derived FG peptides identified CA-N57 as critical for NUP153 and CPSF6 binding; N57 mutant virus infects dividing but not non-dividing cells and shows altered integration site patterns, directly linking the NUP153–CA structural interface to nuclear entry and integration targeting.

    Evidence X-ray crystallography; structure-guided mutagenesis; infectivity assays in dividing vs. non-dividing cells; integration site analysis

    PMID:29997211

    Open questions at the time
    • Whether NUP153 guides integration site selection independently of CPSF6
    • No intact capsid lattice–NUP153 structure
  16. 2023 High

    Cryo-EM resolved NUP153 engagement with assembled CA lattices via a bipartite motif: an FG motif at the hexamer pocket and an RRR motif at the tri-hexamer interface, both required for HIV-1 nuclear import; NUP153 stabilizes tubular CA assemblies, suggesting it maintains capsid integrity during nuclear entry.

    Evidence Cryo-EM of CA assemblies with NUP153 peptides; mutagenesis of FG and RRR motifs; HIV-1 infection assays; in vitro CA stabilization

    PMID:36943880

    Open questions at the time
    • How bipartite binding cooperates with CPSF6 in the intact NPC context
    • Whether NUP153 stabilization of CA tubes occurs inside the NPC channel
  17. 2024 High

    NUP153 was identified as the nuclear envelope anchor for kinesin Kif1a, required for G1-phase basal interkinetic nuclear migration in radial glial progenitors, revealing a cell-cycle-specific cytoskeletal coupling function.

    Evidence Co-immunoprecipitation; siRNA/shRNA knockdown; live-cell imaging of nuclear migration in brain progenitors

    PMID:39666457

    Open questions at the time
    • Whether this function extends to other progenitor types
    • Structural basis of NUP153–Kif1a interaction unknown
  18. 2025 High

    The Cul3–SPOP E3 ubiquitin ligase was identified as a direct regulator of NUP153 turnover, with SPOP binding NUP153 in a multivalent manner to target it for proteasomal degradation; SPOP loss stabilizes NUP153 and increases Mad1 at the nuclear envelope, linking NUP153 protein levels to checkpoint control.

    Evidence Co-IP; ubiquitylation assays; SPOP substrate-binding mutant control; RNAi stabilization

    PMID:39785820

    Open questions at the time
    • SPOP binding sites on NUP153 not mapped
    • Whether SPOP-mediated degradation is cell-cycle regulated
    • Functional consequence for spindle checkpoint fidelity not quantified

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include: how NUP153's transport, chromatin-regulatory, and scaffolding functions are coordinated in space and time; the structural basis of full-length NUP153 interactions with its numerous partners; and whether NUP153 sumoylation, SPOP-mediated turnover, and transcription-coupled mobility are mechanistically linked.
  • No full-length NUP153 structure
  • Functional interplay between sumoylation and ubiquitylation of NUP153 uncharacterized
  • In vivo RNA targets of the NUP153 RNA-binding domain not identified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0003723 RNA binding 3 GO:0005198 structural molecule activity 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005634 nucleus 4 GO:0005635 nuclear envelope 4 GO:0005694 chromosome 2
Pathway
R-HSA-9609507 Protein localization 7 R-HSA-168256 Immune System 5 R-HSA-1640170 Cell Cycle 4 R-HSA-74160 Gene expression (Transcription) 3 R-HSA-8953854 Metabolism of RNA 3 R-HSA-1266738 Developmental Biology 2 R-HSA-4839726 Chromatin organization 2 R-HSA-73894 DNA Repair 2
Partners
KPNB1MAD1L1NUP50SENP1SENP2SOX2TNPO1TPR
Complex memberships
Nuclear pore complex (nuclear basket)Nup107-160 complex (recruiter, not subunit)

Evidence

Reading pass · 46 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1994 Human NUP153 (hnup153) encodes a nucleoporin with 33 copies of the XFXFG pentapeptide repeat, O-linked N-acetylglucosamine modifications, and four zinc finger motifs related to those in mdm-2 and Drosophila small optic lobes, defining its primary structure and domain architecture. cDNA sequence analysis Biochimica et biophysica acta Medium 8110839
1996 Nup153 localizes to the nucleoplasmic face of the nuclear pore complex (NPC) basket via its N-terminal domain, while its C-terminal XFXFG-repeat domain is required for mRNA export; overexpression of Nup153 causes dramatic nuclear accumulation of poly(A)+ RNA without affecting protein import. Overexpression of deletion constructs in BHK cells, fluorescence microscopy of poly(A)+ RNA distribution The Journal of cell biology High 8794857
1998 The N-terminal domain of Nup153 contains two distinct targeting regions: one mediates assembly into the NPC and the other targets proteins to the inner face of the nuclear envelope, while the zinc finger and C-terminal domains have no targeting role. Deletion mutagenesis with reporter (pyruvate kinase) fusion constructs expressed in cells Chromosoma High 9745047
1998 Nup153 is a major physiological binding site for importin β at the nuclear face of the NPC; importin β binds directly to multiple sites within the Nup153 FXFG repeat region, and Nup153 can bind a complete import complex containing importin α, importin β, and an NLS substrate, consistent with a role in the terminal step of nuclear import. Immunoprecipitation from Xenopus egg extracts and isolated nuclei; in vitro binding with purified recombinant proteins The Journal of cell biology High 9531546
1998 Nup153 contains separate binding sites for importin α/β (classical NLS pathway) and transportin (M9 pathway); dominant-negative Nup153 fragments containing each site selectively block the corresponding import pathway without affecting the other. In vitro nuclear import assays in Xenopus oocyte extracts with dominant-negative Nup153 fragments Current biology High 9889100
1999 Nup153 contains an M9 nuclear localization sequence in its N-terminus that binds transportin 1 (TRN1); Nup153 also contains a zinc finger Ran-binding domain that binds RanGDP; Nup153 interacts with both import and export receptors in a RanGTP-regulated fashion (RanGTP dissociates import receptor complexes but is required for export receptor interactions); Nup153 shuttles between nuclear and cytoplasmic faces of the NPC. Phage display screen for TRN1 interactors; co-immunoprecipitation; RanGTP-regulated binding assays; in vitro transport assays The EMBO journal High 10202161
1999 Nup153 is required for nuclear export of snRNA, mRNA, 5S rRNA, and NES-protein (HIV Rev) export pathways but not for tRNA export or importin β recycling; Nup153 can directly associate with poly(G) and poly(U) RNA in vitro, suggesting an RNA-binding capacity unique among tested nucleoporins. Anti-Nup153 antibody microinjection into Xenopus oocytes; RNA export assays; homoribopolymer binding assays Molecular biology of the cell High 10069809
2000 Nup153 incorporation into the nuclear envelope requires prior lamina assembly; lamin B3 specifically co-immunoprecipitates with Nup153 via the C-terminal domain of Nup153; preventing lamina assembly blocks Nup153 recruitment while other nucleoporins assemble normally. Co-immunoprecipitation of in vitro translated proteins; Xenopus cell-free nuclear assembly with dominant-negative lamin mutant; immunofluorescence The EMBO journal High 10921874
2000 Nup153 localizes to the nuclear ring of the NPC (basket base); NPCs assembled without Nup153 lack nuclear basket components, are unevenly distributed and mobile within the nuclear envelope (not anchored), and show strongly reduced importin α/β-mediated import while transportin-mediated import is unaffected. Immunogold electron microscopy; Xenopus egg extract nuclear reconstitution with Nup153 immunodepletion; nuclear transport assays The EMBO journal High 11598013
2000 During telophase in living HeLa cells, Nup153 is recruited to reforming nuclear envelopes very early (along with emerin, LBR, and RanBP2), prior to recovery of nuclear import function, establishing the temporal order of NPC reassembly. Live fluorescence imaging of GFP-tagged nuclear envelope proteins in HeLa cells; immunofluorescence at precise mitotic time points Journal of cell science Medium 10671368
2001 Nup153 contains a novel RNA binding domain mapping to amino acids 250–400 that directly binds RNA; this domain is functionally conserved across Drosophila, Xenopus, and human Nup153, and recombinant Nup153 fragments interact with endogenous RNA targets. In vitro RNA binding assays with recombinant Nup153 fragments; cross-species domain analysis The Journal of biological chemistry High 11567018
2002 Smad2 directly interacts with nucleoporins CAN/Nup214 and Nup153; these interactions mediate constitutive nucleocytoplasmic shuttling of Smad2 and compete with binding to the cytoplasmic retention factor SARA and nuclear partner FAST-1 via a hydrophobic corridor on Smad2 MH2 domain; TGFβ receptor phosphorylation does not affect Smad2 affinity for Nup153 but alters its interactions with SARA and Smad4. Direct protein interaction assays; competition binding experiments; nuclear accumulation assays in TGFβ-stimulated cells Molecular cell High 12191473
2003 Nup153 directly binds Tpr (a nuclear filament protein) and is required for Tpr localization to the NPC periphery; in the absence of Nup153 (via RNAi), Tpr mislocalizes to the nuclear interior; depletion of Nup153 also causes mislocalization of Nup50; the specificity of the Nup153–Tpr interaction is confirmed by Tpr mutations that abolish NPC binding and eliminate direct Nup153 binding. RNAi depletion; affinity chromatography; yeast two-hybrid interaction studies; immunofluorescence Molecular biology of the cell High 12802065
2003 Nup153 recruits the COPI coatomer complex to the nuclear membrane at mitosis via its zinc finger domain, thereby directing nuclear envelope breakdown; this involves vesiculation as an important step and COPI recruitment provides feedback to other aspects of nuclear disassembly. Xenopus egg extract nuclear envelope breakdown assay; immunodepletion; functional rescue experiments Developmental cell High 12967567
2004 Nup153 is a dynamic (mobile) nucleoporin that exchanges on and off the NPC in a transcription-dependent manner; its exchange is inhibited when RNA Pol I and Pol II transcription is blocked; distinct domains control NPC localization versus transcription-coupled mobility. Fluorescence recovery after photobleaching (FRAP) of GFP-Nup153 in live cells; transcription inhibitors; deletion analysis Molecular biology of the cell High 14718558
2004 The Nup153 RNA binding domain (amino acids 250–400) associates preferentially with single-stranded RNA with little sequence preference. In vitro RNA binding assays testing diverse RNA substrates with purified recombinant Nup153 RBD fragment RNA Medium 14681581
2005 PU.1 undergoes carrier-independent nuclear import requiring energy and direct interaction with Nup153; RanGTP dramatically increases PU.1 binding to Nup153 (forming a PU.1·RanGTP·Nup153 complex), suggesting RanGTP propels PU.1 toward the nuclear basket; gold-labeled PU.1 accumulates at the nuclear side of the pore in permeabilized cells. GFP-PU.1 transport assays; direct binding assays with purified Nup153 and Nup62; immunoelectron microscopy The Journal of biological chemistry High 15632149
2005 Nup153 zinc finger domain binds the COPI complex and is required for nuclear envelope breakdown; both Nup153 and Nup358/RanBP2 zinc finger domains independently recruit COPI to the NPC and play non-redundant roles (cytoplasmic and nuclear faces) in coordinating nuclear envelope disassembly. Xenopus extract nuclear envelope breakdown assay; dominant-negative zinc finger domain expression; COPI binding assays; antibody inhibition Molecular biology of the cell High 16314393
2007 The Nup153 RNA binding domain discriminates between RNA targets via recognition of a loose sequence motif, preferentially binding specific subregions of mRNA over structured RNAs (tRNA, snRNA, dsRNA), indicating sequence-dependent rather than purely general single-stranded RNA recognition. Systematic in vitro binding assays with synthetic RNA oligonucleotides; mapping binding determinants within cellular mRNA fragments The Journal of biological chemistry Medium 17242408
2007 In Drosophila, the FG repeats of Nup153 are necessary for its function in importin α/β-mediated nuclear import, while the non-FG portion of Nup153 maintains pore integrity; Nup153 is selectively required for import but not CRM1-dependent export. RNAi knockdown of nucleoporins in Drosophila S2 cells; quantitative import and export assays; domain rescue experiments The Journal of cell biology High 17682050
2009 HIV-1 integrase (IN) directly binds the FxFG-rich C-terminal domain of NUP153 (NUP153C); this interaction mediates nuclear import of IN independently of classical Ran-dependent pathways; excess NUP153C inhibits IN nuclear import and reduces HIV-1 vector infectivity by interfering with viral cDNA nuclear translocation. Semi-permeabilized cell nuclear import assay; direct binding assay between purified IN and NUP153C; overexpression competition experiment Journal of virology High 19369352
2009 Nup153 depletion by RNAi delays the late stages of mitosis and increases unresolved midbodies; more severe depletion causes multilobed nuclei accumulation early in mitosis; the FG-rich domain of Nup153 is specifically required to rescue late mitotic defects, while rescue of multilobed nuclei is FG-domain-independent, revealing two separable mitotic roles. siRNA knockdown in HeLa cells; live cell imaging; domain rescue with Nup153 deletion constructs Molecular biology of the cell High 19158386
2010 In Drosophila, Nup153 and Megator bind continuously to 25% of the genome in large domains (10 kb–500 kb, called NARs) enriched for active transcription marks (high RNA Pol II, H4K16ac); RNAi knockdown of Nup153 alters expression of ~5,700 genes with pronounced downregulation within NARs; Nup153 depletion abolishes dosage compensation complex function on the male X chromosome, and this regulation occurs independent of nuclear periphery localization. ChIP-chip (chromatin immunoprecipitation + microarray); RNAi knockdown; expression profiling; 3D imaging PLoS genetics High 20174442
2010 Nup153 directly binds Mad1 (spindle assembly checkpoint protein) via its N-terminal domain; overexpression of Nup153 induces multinucleated cells, multipolar spindles, and spindle checkpoint inactivation through Mad1 hypophosphorylation; depletion of Nup153 causes Mad1 loss from nuclear pores during interphase and delayed Mad1 dissociation from kinetochores in metaphase, keeping the checkpoint active. In vitro binding assay (direct Mad1-Nup153 binding); RNAi knockdown; overexpression in HeLa cells; immunofluorescence Nucleus High 21327106
2010 Nup153 depletion by RNAi disrupts nuclear lamina organization, mislocalizes Sun1, and causes dramatic cytoskeletal rearrangement that impairs cell migration in human breast carcinoma cells. RNAi knockdown; immunofluorescence for lamins and Sun1; cell migration assays FEBS letters Medium 20561986
2011 HIV-1 capsid (CA) protein determines the requirement for NUP153 during infection; CA mutants N74D and P90A are largely insensitive to NUP153 depletion; cyclophilin A depletion or cyclosporine A treatment also relieves NUP153 dependency; NUP153 knockdown causes a reduction in 2-LTR circles and large reduction in integrated proviruses, suggesting NUP153 function is at the nuclear import step of the viral preintegration complex. siRNA knockdown; HIV-1/MLV chimera viruses; CA missense mutants; quantitative PCR for viral integration intermediates Journal of virology High 21593146
2011 Nup153 interacts with A-type (lamin A/C) and B-type lamins through multiple binding sites: both its N-terminal domain and C-terminal domain associate with the Ig-fold domain of lamins; mutations in the lamin A Ig-fold selectively abolish Nup153 binding. GST pull-down assays; blot overlay assays with purified proteins; lamin mutant binding analysis Nucleus High 21983083
2011 NUP153 knockdown specifically prevents 53BP1 nuclear import in newly forming daughter cells without blocking nuclear import of other DNA damage response factors; the C-terminal part of NUP153 is required for 53BP1 nuclear import; 53BP1 import involves an NUP153–importin-β interplay. siRNA screen; live-cell imaging; cell and molecular biology approaches including fractionation; domain mapping Cell death and differentiation High 22075984
2011 β-catenin Arm repeats R3-8 and R10-12 directly interact in vitro with FG repeats of Nup153 (as well as Nup62 and Nup98), enabling Ran/transport receptor-independent NPC traversal; knockdown of Nup153 (and Nup62/Nup358) impedes β-catenin nuclear import/export rate. FRAP in living cells; in vitro binding with purified components; proteomics screen (RanBP2/Nup358 identification); siRNA knockdown The Journal of biological chemistry High 22110128
2012 Nup153 scaffolds Nup50 at the NPC via a dual interface: (1) the unique N-terminal domain of Nup153 is critical for Nup50 pore localization; (2) a second site in the Nup153 C-terminal FG region is importin α-dependent; disruption of the Nup153–Nup50 interface decreases nuclear import efficiency. Deletion mutagenesis; co-immunoprecipitation; nuclear import assays; rescue experiments The Journal of biological chemistry High 23007389
2012 Nup153 interacts with SUMO proteases SENP1 and SENP2 at two distinct sites (N-terminal domain and C-terminal FG region); Nup153 itself is a substrate for sumoylation and this modification is kept in check by SENP1/SENP2; SENP1 levels are regulated by Nup153 abundance, while SENP2 is not sensitive to Nup153 levels. Co-immunoprecipitation; RNAi depletion; dominant-negative SENP expression; sumoylation assays for endogenous Nup153 Nucleus High 22688647
2013 The FG-repeat-enriched C-terminal domain of NUP153 directly binds the N-terminal domain of HIV-1 capsid (CA) protein; this interaction maps to the CA α-helix 3/4 hydrophobic pocket also targeted by CPSF6 and PF74; different FG motifs mediate HIV-1 versus EIAV capsid binding; PF74 and CPSF6 compete with NUP153(C) for the same CA pocket; the NUP153(C)–CA interaction underlies HIV-1 infection of non-dividing cells. Trim-NUP153(C) restriction assay (intracellular binding readout); direct binding assays with purified proteins; mutagenesis of NUP153(C) and CA; competition assays; cell-cycle dependency experiments PLoS pathogens High 24130490
2015 Nup153 depletion in mouse embryonic stem cells causes derepression of developmental genes and induction of differentiation; Nup153 binds around the transcriptional start site of developmental genes and mediates recruitment of Polycomb Repressive Complex 1 (PRC1) to a subset of its target loci; this epigenetic silencing function is not mediated through nuclear import of pluripotency factors. RNAi knockdown; ChIP-seq; gene expression analysis; PRC1 recruitment assays Genes & development High 26080816
2015 Nup153 is required for NPC assembly during interphase but not during mitotic exit; it functions in interphasic NPC formation by binding directly to the inner nuclear membrane via an N-terminal amphipathic helix; this membrane binding facilitates recruitment of the Nup107-160 complex to assembly sites; transportin and Ran regulate the Nup153–membrane interaction to direct NPC assembly during interphase. siRNA knockdown; in vitro membrane binding assay; domain mutagenesis; co-immunoprecipitation; live-cell imaging Developmental cell High 26051542
2016 Prelamin A accumulation mislocalizes NUP153, disrupts the Ran gradient (NUP153 is required for nuclear Ran localization), and thereby impairs nuclear import of 53BP1, causing defective DNA damage response in vascular smooth muscle cells. Immunofluorescence; nuclear fractionation; siRNA and overexpression in cells expressing prelamin A; small molecule rescue (Remodelin) Aging cell Medium 27464478
2017 Nup153 interacts directly with Sox2 in adult neural progenitor cells; genome-wide binding shows Nup153 and Sox2 co-regulate hundreds of genes; Nup153 binding at gene promoters correlates with increased expression while binding at transcriptional end sites correlates with decreased expression; Nup153 depletion disrupts Sox2 genomic localization and promotes differentiation in vitro and a gliogenic fate switch in vivo. Co-immunoprecipitation; ChIP-seq; ATAC-seq (open chromatin); shRNA knockdown; in vitro and in vivo differentiation assays Cell stem cell High 28919367
2017 Nup153 (with Nup50) promotes 53BP1 recruitment to DNA double-strand break foci independently of its role in 53BP1 nuclear import; this recruitment function requires antagonism of BRCA1/BARD1-mediated events and places Nup153 and Nup50 in the molecular pathway regulating NHEJ vs. HR pathway choice. siRNA knockdown; DSB focus formation assays (etoposide, olaparib); epistasis with BRCA1/BARD1/BRCA2 knockdown Journal of cell science Medium 28751496
2017 Nup153 localizes SENP1 to nuclear pores; loss of Nup153 displaces SENP1, reduces 53BP1 sumoylation (a prerequisite for efficient 53BP1 accumulation at DSBs), and impairs NHEJ; artificial tethering of SENP1 to NPCs in the absence of Nup153 restores NHEJ and 53BP1 sumoylation. siRNA knockdown; artificial SENP1 tethering; NHEJ reporter assay; SUMO modification assays Journal of cell science High 28576968
2018 Crystal structures of hexameric HIV-1 capsid in complex with NUP153-derived FG-repeat peptides guided mutagenesis; HIV-1 capsid N57 residue is critical for interaction with both NUP153 and CPSF6; N57 mutant HIV-1 infects dividing but not non-dividing cells, undergoes reverse transcription but not nuclear translocation, and shows diminished integration into transcriptionally active genes resembling CPSF6 knockout patterns. X-ray crystallography; structure-based mutagenesis; infectivity assays in dividing vs. non-dividing cells; integration site analysis Journal of virology High 29997211
2018 Seh1 is required for the association of Nup153 (and GATOR2) with mitotic chromosomes but is not needed for Nup107 complex chromosome association, revealing a Seh1-dependent pathway for Nup153 mitotic chromosome targeting. Chemical genetics (auxin-inducible degron); quantitative chromosome proteomics; immunofluorescence Journal of cell science Medium 29618633
2020 Mad1 depletion delays recruitment of Nup153 to anaphase chromatin and prolongs anaphase; the Nup153–Mad1 association requires a nuclear envelope to be present; both Nup153 and Mad1 depletion alter NPC architecture (membrane curvature and inner/outer nuclear membrane spacing); Nup153 depletion also causes interphase NPC assembly defects independent of Mad1. siRNA depletion; in situ proximity ligation assay; time-lapse microscopy; electron microscopy; 3D-SIM Journal of cell science High 33023979
2022 Disrupting Nup153 function during telophase impairs ongoing addition of B-type lamins, lamin B receptor, and SUN1 to the expanding nuclear envelope after initial chromatin enclosure, while lamin A and SUN2 recruitment is minimally affected; this reveals two functionally separable phases of nuclear envelope formation in mammalian cells with Nup153 acting in the expansion phase. siRNA knockdown; dominant-negative Nup153 constructs; live-cell imaging; immunofluorescence during telophase Molecular biology of the cell High 36044344
2023 NUP153 engages assembled HIV-1 CA lattice through a bipartite motif: a canonical FG motif that binds the CA hexamer, and a newly identified triple-arginine (RRR) motif that targets the CA tri-hexamer interface; both motifs are required for HIV-1 nuclear import; NUP153 stabilizes tubular CA assemblies in vitro. Cryo-EM structure of CA assemblies with NUP153 peptides; mutagenesis; HIV-1 infection assays; in vitro CA assembly stabilization assay Proceedings of the National Academy of Sciences High 36943880
2023 RTEL1 interacts with NUP153 through a distinct C-terminal domain; this interaction contributes to nuclear internalization of peptides; RTEL1 overexpression protects against nuclear envelope anomalies caused by protein import inhibition in an S-phase-specific manner. Co-immunoprecipitation; domain deletion mapping; nuclear transport assays with peptides; live-cell high-resolution microscopy Cells Medium 38132118
2024 Nup153 is the nucleoporin anchor for the kinesin Kif1a at the nuclear envelope, required for G1-specific basal nuclear migration (interkinetic nuclear migration) in radial glial progenitor cells; this interaction is specific to G1 phase basal migration. Co-immunoprecipitation; siRNA/shRNA knockdown; live-cell imaging of nuclear migration in brain progenitors Cell reports High 39666457
2025 SPOP (a Cul3 E3 ligase substrate adaptor) directly binds Nup153 in a multivalent manner and targets it for ubiquitylation and proteasomal degradation; SPOP depletion stabilizes Nup153; loss of SPOP activity increases Mad1 localization at the nuclear envelope (which depends on Nup153 tethering); SPOP-F102C (substrate-binding-deficient mutant) cannot degrade Nup153. Co-immunoprecipitation; colocalization; ubiquitylation assay; RNAi stabilization; domain mutagenesis Molecular biology of the cell High 39785820

Source papers

Stage 0 corpus · 66 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2013 Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity. PLoS pathogens 246 24130490
2002 Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFbeta signaling complexes in the cytoplasm and nucleus. Molecular cell 206 12191473
2010 Nuclear pore proteins nup153 and megator define transcriptionally active regions in the Drosophila genome. PLoS genetics 205 20174442
1999 Nup153 is an M9-containing mobile nucleoporin with a novel Ran-binding domain. The EMBO journal 198 10202161
2011 The requirement for nucleoporin NUP153 during human immunodeficiency virus type 1 infection is determined by the viral capsid. Journal of virology 187 21593146
2001 The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins. The EMBO journal 187 11598013
1996 Targeting and function in mRNA export of nuclear pore complex protein Nup153. The Journal of cell biology 167 8794857
1998 Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr. The Journal of cell biology 166 9531546
2000 Live fluorescence imaging reveals early recruitment of emerin, LBR, RanBP2, and Nup153 to reforming functional nuclear envelopes. Journal of cell science 160 10671368
2003 Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex. Molecular biology of the cell 152 12802065
2015 The nucleoporin Nup153 regulates embryonic stem cell pluripotency through gene silencing. Genes & development 128 26080816
1999 The nucleoporin nup153 plays a critical role in multiple types of nuclear export. Molecular biology of the cell 119 10069809
2000 Incorporation of the nuclear pore basket protein nup153 into nuclear pore structures is dependent upon lamina assembly: evidence from cell-free extracts of Xenopus eggs. The EMBO journal 118 10921874
2015 Nup153 Recruits the Nup107-160 Complex to the Inner Nuclear Membrane for Interphasic Nuclear Pore Complex Assembly. Developmental cell 115 26051542
1998 Separate nuclear import pathways converge on the nucleoporin Nup153 and can be dissected with dominant-negative inhibitors. Current biology : CB 108 9889100
2017 Nup153 Interacts with Sox2 to Enable Bimodal Gene Regulation and Maintenance of Neural Progenitor Cells. Cell stem cell 96 28919367
2004 Distinct functional domains within nucleoporins Nup153 and Nup98 mediate transcription-dependent mobility. Molecular biology of the cell 95 14718558
2018 Nup153 Unlocks the Nuclear Pore Complex for HIV-1 Nuclear Translocation in Nondividing Cells. Journal of virology 94 29997211
2009 Integrase interacts with nucleoporin NUP153 to mediate the nuclear import of human immunodeficiency virus type 1. Journal of virology 90 19369352
2005 Versatility at the nuclear pore complex: lessons learned from the nucleoporin Nup153. Chromosoma 74 16133350
2011 Distinct association of the nuclear pore protein Nup153 with A- and B-type lamins. Nucleus (Austin, Tex.) 71 21983083
2009 The nucleoporin Nup153 has separable roles in both early mitotic progression and the resolution of mitosis. Molecular biology of the cell 68 19158386
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
2003 The COPI complex functions in nuclear envelope breakdown and is recruited by the nucleoporin Nup153. Developmental cell 65 12967567
2011 Nucleoporin NUP153 guards genome integrity by promoting nuclear import of 53BP1. Cell death and differentiation 61 22075984
2012 The Nup153-Nup50 protein interface and its role in nuclear import. The Journal of biological chemistry 51 23007389
2007 Distinct functions of the Drosophila Nup153 and Nup214 FG domains in nuclear protein transport. The Journal of cell biology 51 17682050
2010 The nucleoporin Nup153 affects spindle checkpoint activity due to an association with Mad1. Nucleus (Austin, Tex.) 50 21327106
2010 The nucleoporin Nup153 maintains nuclear envelope architecture and is required for cell migration in tumor cells. FEBS letters 48 20561986
2016 Prelamin A impairs 53BP1 nuclear entry by mislocalizing NUP153 and disrupting the Ran gradient. Aging cell 46 27464478
1998 Amino-terminal sequences that direct nucleoporin nup153 to the inner surface of the nuclear envelope. Chromosoma 43 9745047
2005 Nuclear envelope breakdown is coordinated by both Nup358/RanBP2 and Nup153, two nucleoporins with zinc finger modules. Molecular biology of the cell 41 16314393
1994 Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153. Biochimica et biophysica acta 41 8110839
2012 Two distinct sites in Nup153 mediate interaction with the SUMO proteases SENP1 and SENP2. Nucleus (Austin, Tex.) 38 22688647
2005 Carrier-independent nuclear import of the transcription factor PU.1 via RanGTP-stimulated binding to Nup153. The Journal of biological chemistry 38 15632149
2023 The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores. Proceedings of the National Academy of Sciences of the United States of America 35 36943880
2019 Altered Nup153 Expression Impairs the Function of Cultured Hippocampal Neural Stem Cells Isolated from a Mouse Model of Alzheimer's Disease. Molecular neurobiology 35 30689197
2005 The functionally conserved nucleoporins Nup124p from fission yeast and the human Nup153 mediate nuclear import and activity of the Tf1 retrotransposon and HIV-1 Vpr. Molecular biology of the cell 35 15659641
2014 Structural characterization of altered nucleoporin Nup153 expression in human cells by thin-section electron microscopy. Nucleus (Austin, Tex.) 32 25485891
2005 Nup153 affects entry of messenger and ribosomal ribonucleoproteins into the nuclear basket during export. Molecular biology of the cell 32 16195343
2017 Localisation of Nup153 and SENP1 to nuclear pore complexes is required for 53BP1-mediated DNA double-strand break repair. Journal of cell science 30 28576968
2001 RNA association defines a functionally conserved domain in the nuclear pore protein Nup153. The Journal of biological chemistry 20 11567018
2017 Nup153 and Nup50 promote recruitment of 53BP1 to DNA repair foci by antagonizing BRCA1-dependent events. Journal of cell science 19 28751496
2000 Recombinant Nup153 incorporates in vivo into Xenopus oocyte nuclear pore complexes. Journal of structural biology 17 10806081
2018 Seh1 targets GATOR2 and Nup153 to mitotic chromosomes. Journal of cell science 16 29618633
2007 Multiple conserved domains of the nucleoporin Nup124p and its orthologs Nup1p and Nup153 are critical for nuclear import and activity of the fission yeast Tf1 retrotransposon. Molecular biology of the cell 14 17615301
2007 Sequence preference in RNA recognition by the nucleoporin Nup153. The Journal of biological chemistry 13 17242408
2004 The RNA binding domain within the nucleoporin Nup153 associates preferentially with single-stranded RNA. RNA (New York, N.Y.) 11 14681581
2022 NUP153 promotes HCC cells proliferation via c-Myc-mediated downregulation of P15INK4b. Digestive and liver disease : official journal of the Italian Society of Gastroenterology and the Italian Association for the Study of the Liver 9 35288064
2022 A role for Nup153 in nuclear assembly reveals differential requirements for targeting of nuclear envelope constituents. Molecular biology of the cell 8 36044344
2020 Mitotic checkpoint protein Mad1 is required for early Nup153 recruitment to chromatin and nuclear envelope integrity. Journal of cell science 5 33023979
2025 Cul3 substrate adaptor SPOP targets Nup153 for degradation. Molecular biology of the cell 4 39785820
2024 Nup153 is not required for anchoring heterochromatic DSBs to the nuclear periphery. microPublication biology 4 38737725
2023 Human RTEL1 Interacts with KPNB1 (Importin β) and NUP153 and Connects Nuclear Import to Nuclear Envelope Stability in S-Phase. Cells 4 38132118
2021 Expression of NR5A2, NUP153, HNF4A, USP15 and FNDC3B is consistent with their use as novel biomarkers for bovine mammary stem/progenitor cells. Journal of molecular histology 4 33400051
2020 Viral protein X unlocks the nuclear pore complex through a human Nup153-dependent pathway to promote nuclear translocation of the lentiviral genome. Molecular biology of the cell 4 31913756
2025 Nup358 and Nup153 Facilitate nuclear import of BmNPV nucleocapsids in Bombyx mori cells. Journal of invertebrate pathology 3 40120667
2022 Effect of Genetic Polymorphism Including NUP153 and SVEP1 on the Pharmacokinetics and Pharmacodynamics of Ticagrelor in Healthy Chinese Subjects. Clinical drug investigation 3 35501592
2025 The role of ABI2 in modulating nuclear proteins: Therapeutic implications for NUP54 and NUP153 in TNBC. Advances in protein chemistry and structural biology 2 39843146
2025 Novel Function of NUP153 in HNF4α Transcriptional Upregulation Contributes to Promoting HBV Replication. Journal of medical virology 2 40014546
2025 The functional and clinical significance of nucleoporin NUP153 across human cancers: a systematic study based on multi-omics analysis and bench work validation. Frontiers in immunology 2 40607419
2026 Proviral NUP153 binding to viral proteins and RNA regulates structural-nonstructural protein ratios in orthoflavivirus infection. Nature communications 0 41951628
2025 Nup153 and TPR/Megator Interact with TREX-2 Subunits and Are Essential for TREX-2-Dependent Nuclear Export of hsp70 mRNA in Drosophila. International journal of molecular sciences 0 40943515
2024 The nucleoporin Nup153 is the anchor for Kif1a during basal nuclear migration in brain progenitor cells. Cell reports 0 39666457
2023 Expression of the NUP153 and YWHAB genes from their canonical promoters and alternative promoters of the LINE-1 retrotransposon in the placenta of the first trimester of pregnancy. Vavilovskii zhurnal genetiki i selektsii 0 36923475
2023 Cul3 substrate adaptor SPOP targets Nup153 for degradation. bioRxiv : the preprint server for biology 0 37293018