Affinage

NUP188

Nucleoporin NUP188 · UniProt Q5SRE5

Round 2 corrected
Length
1749 aa
Mass
196.0 kDa
Annotated
2026-04-29
66 papers in source corpus 21 papers cited in narrative 21 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NUP188 encodes a large scaffold nucleoporin that serves as a question-mark-shaped keystone of the nuclear pore complex (NPC) inner ring, where it establishes structural integrity, sets the resting diameter of the central transport channel, and enables NPC constriction–dilation dynamics through a linker–scaffold network with Nic96/Nup93, Nup205, Pom152, and linker nucleoporins (PMID:8682855, PMID:10831607, PMID:35679425). Its NTR-like fold binds FG-repeat domains and allows facilitated diffusion through the NPC, blurring the classical distinction between stationary scaffold and mobile transport factors (PMID:23795296, PMID:29033133). Beyond the NPC, NUP188 localizes to centrosomes where it directly binds Cep152 to promote centriole duplication, to mitotic spindle poles where it recruits NuMA for K-fiber formation, and to the nuclear periphery where it participates with Nup93 in HOXA gene cluster repression (PMID:32211895, PMID:23551833, PMID:27980680). NUP188 is also required for left–right body axis patterning in Xenopus, likely via cilia-dependent signaling (PMID:21282601).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 1995 High

    The initial question—what are the principal mass components of the NPC scaffold?—was addressed by direct microsequencing of isolated yeast NPCs, which identified Nup188 as constituting a major fraction of total NPC mass and revealed synthetic lethal interactions with POM152 and NUP170, establishing Nup188 within a redundant structural scaffold network.

    Evidence Microsequencing of purified yeast NPC fractions combined with synthetic lethal screens in S. cerevisiae

    PMID:8522578

    Open questions at the time
    • Precise stoichiometry and position of Nup188 within the NPC were not resolved
    • Vertebrate ortholog was not yet identified
  2. 1996 High

    The question of where Nup188 sits within the NPC and which partners anchor it was resolved by immuno-EM localizing Nup188 to both faces of the NPC core and by demonstrating direct physical interactions with Nic96p and Pom152p, defining the inner-ring Nic96–Nup188 axis as a central organizational module.

    Evidence Immuno-electron microscopy, affinity purification (ProtA-Nup188p), allele-specific genetic interaction analysis in S. cerevisiae

    PMID:8682854 PMID:8682855

    Open questions at the time
    • Structural basis of Nic96–Nup188 interaction was unknown
    • Contribution of Nup188 to transport selectivity was not measured
  3. 1999 Medium

    The functional requirement for the Pom152 lumenal domain in rescuing nup188 mutations, and the genetic connection between Nup188 deletion and Hsp70-assisted import, together established that Nup188 functionally bridges the pore membrane and the transport machinery.

    Evidence Domain complementation assays of Pom152 in nup188 mutant backgrounds; genetic suppression of nup188Δ import defects by Ssa1p overexpression in S. cerevisiae

    PMID:10347213 PMID:9988776

    Open questions at the time
    • Direct binding interface between Nup188 and the Pom152 lumenal domain was not mapped
    • Mechanism by which Hsp70 suppresses nup188Δ transport defects was not resolved
  4. 2000 High

    The question of whether Nup188 has a functional role in transport selectivity—beyond passive scaffolding—was answered: nup188Δ cells show an enlarged NPC diffusion channel, demonstrating that Nup188 is a determinant of the NPC's size-exclusion barrier.

    Evidence Quantitative in vivo fluorescence transport assays with NLS/NES-GFP reporters of varying sizes in nup188Δ S. cerevisiae; identification of vertebrate Nup188 in Xenopus extract NPC assemblies

    PMID:10831607 PMID:11029043

    Open questions at the time
    • How Nup188 physically restricts channel diameter was structurally undefined
    • Vertebrate Nup188 function in transport had not been tested
  5. 2011 Medium

    Whether NUP188 functions outside nucleocytoplasmic transport was an open question; morpholino knockdown in Xenopus revealed a requirement for NUP188 in left–right body patterning, likely via cilia at the gastrocoel roof plate, extending NUP188 biology to developmental signaling.

    Evidence Morpholino knockdown in Xenopus embryos with pitx2 in situ hybridization and LR morphological scoring

    PMID:21282601

    Open questions at the time
    • Direct ciliary localization of Nup188 in the LR organizer was not shown
    • Whether the phenotype is NPC-dependent or NPC-independent was not resolved
  6. 2013 High

    Two landmark studies resolved the structure and an unexpected NPC-external function: the crystal structure revealed an NTR-like fold that binds FG-repeats and enables NPC translocation, while RNAi in human cells showed spindle-pole localization during mitosis with NuMA recruitment enabling K-fiber formation—establishing Nup188 as both a scaffold and a mobile, multifunctional protein.

    Evidence X-ray crystallography of yeast Nup188 with FG-repeat binding and in vivo translocation assays; RNAi knockdown with live-cell imaging, co-IP (Nup188–NuMA), and K-fiber analysis in human cells

    PMID:23551833 PMID:23795296

    Open questions at the time
    • Atomic-resolution structure of full-length vertebrate NUP188 was lacking
    • Whether mitotic and interphase pools are independently regulated was unknown
  7. 2016 Medium

    The discovery that depletion of Nup188 (as part of the Nup93 sub-complex) derepresses the HOXA gene cluster and displaces it from the nuclear periphery established a chromatin-regulatory role, answering whether inner-ring nucleoporins participate in gene silencing.

    Evidence siRNA knockdown with ChIP for histone marks, 3D-FISH for locus positioning, RT-qPCR in human cells

    PMID:27980680

    Open questions at the time
    • Whether Nup188 contributes independently of Nup93 to HOXA repression was not isolated
    • Genome-wide scope of Nup188 chromatin regulation was not assessed
  8. 2018 High

    Multiple studies consolidated the NPC assembly and transport roles: FG-repeat 'Velcro' linkages with Nup188 stabilize late NPC assembly, Brl1 transiently recruits Nup188 during NPC biogenesis, compositional plasticity between Nup188 and Nup192 was quantified, and a cold-sensitive allele linked Nup188 to both protein import and mRNA export pathways.

    Evidence In vitro FG-repeat binding plus genetic epistasis (Cell); co-IP and split-YFP with Brl1 (JCB); quantitative fluorescence NuRIM (PNAS); cold-sensitive allele transport assays (G3), all in S. cerevisiae

    PMID:29033133 PMID:29439116 PMID:29632211 PMID:30021831

    Open questions at the time
    • Temporal order of scaffold assembly involving Nup188 was not fully resolved
    • Whether Nup188/Nup192 plasticity exists in metazoans was not tested
  9. 2020 High

    The centrosomal function of Nup188 was mechanistically dissected: newly synthesized Nup188 populates the pericentriolar material independently of NPC pools, directly binds Cep152, and is required for Sas6 loading during centriole duplication, with differential proteasomal degradation segregating centrosomal and NPC pools.

    Evidence Pulse-chase fluorescent labeling, BioID proximity labeling, super-resolution microscopy, direct binding assays (Nup188–Cep152), Sas6 loading assays upon Nup188 depletion in human cells

    PMID:32211895

    Open questions at the time
    • Structural basis of Nup188–Cep152 binding was not determined
    • Whether the centrosomal pool contributes to congenital heart disease mechanisms in vivo remains to be established in animal models
  10. 2022 High

    High-resolution cryo-EM structures of Nup188 bound to linker nucleoporins defined it as the question-mark-shaped keystone of two hetero-octameric inner-ring complexes, and docking into cryo-ET maps of constricted/dilated NPCs explained how the linker–scaffold network permits inner-ring dilation; separately, Nup188 was shown to bridge the LINC complex (Nesprin-2) to the NPC for SV40 virus nuclear entry.

    Evidence Single-particle cryo-EM and X-ray crystallography with cryo-ET docking and structure-guided mutagenesis in S. cerevisiae (Science); co-IP and siRNA knockdown with viral infection assays in human cells (PLoS Pathog)

    PMID:35679425 PMID:36067270

    Open questions at the time
    • Full in situ structure of the human NPC inner ring at atomic resolution was not achieved
    • Generality of the LINC–NPC handoff to non-viral cargoes was untested
  11. 2025 Medium

    A genome-wide screen identified Nup188 as required for break-induced replication (BIR) completion at a step after DNA synthesis, expanding its roles to DNA repair and placing it sequentially downstream of the Nup84 outer-ring complex in BIR.

    Evidence Genome-wide genetic screen for BIR deficiency with epistasis validation in S. cerevisiae

    PMID:41398407

    Open questions at the time
    • Molecular mechanism by which Nup188 supports BIR completion is unknown
    • Whether this reflects a transport-dependent or NPC-tethering-dependent role was not distinguished

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: (1) the atomic-resolution in situ architecture of metazoan NPC inner rings containing NUP188, (2) the structural basis of Nup188's centrosomal interactions and whether centriole duplication defects underlie congenital heart disease in vivo, (3) whether chromatin-regulatory and BIR functions are NPC-scaffold-dependent or reflect moonlighting of soluble Nup188 pools, and (4) the mechanism linking NUP188 to left–right patterning.
  • No in situ atomic-resolution metazoan NPC structure with NUP188 resolved
  • Centrosomal function not validated in animal disease models
  • Chromatin and BIR mechanisms not dissected from NPC transport functions

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 5 GO:0008092 cytoskeletal protein binding 1
Localization
GO:0005635 nuclear envelope 5 GO:0005815 microtubule organizing center 2 GO:0005634 nucleus 1
Pathway
R-HSA-1852241 Organelle biogenesis and maintenance 3 R-HSA-9609507 Protein localization 3 R-HSA-1640170 Cell Cycle 2 R-HSA-73894 DNA Repair 1 R-HSA-74160 Gene expression (Transcription) 1
Partners
BRL1CEP152NIC96NUMA1NUP205NUP93POM152SYNE2
Complex memberships
NPC inner ring complex (Nup93 sub-complex)Nup93–Nup188–Nup205 complex

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1996 Yeast Nup188p was identified as a major constituent of the NPC, localizing to both cytoplasmic and nucleoplasmic faces of the NPC core. It physically interacts with the pore membrane protein Pom152p and the nucleoporin Nic96p. Null mutants appear normal, but certain dominant alleles cause NPC-associated nuclear envelope herniations and growth inhibition at 37°C. Depletion of Pom152p in nup188 null cells causes severe nuclear envelope deformations, establishing Nup188p as part of the octagonal core structure involved in NPC structural organization. Immunoelectron microscopy, immunofluorescence, co-fractionation with isolated NPCs, genetic interaction analysis (synthetic lethality), dominant allele phenotypic analysis The Journal of cell biology High 8682855
1996 The C-terminal domain of Nic96p functionally interacts with Nup188p in an allele-specific fashion; affinity purification of ProtA-Nup188p co-precipitated a fraction of Nic96p, establishing a physical interaction. Thermosensitive Nic96p mutations in its central domain inhibit NPC formation, and null mutants of NUP188 exhibit striking abnormalities in nuclear envelope and NPC morphology, placing Nup188p in the Nic96p-anchored structural network of the NPC. Allele-specific genetic interaction analysis, affinity purification (ProtA-Nup188p), electron microscopy of nuclear envelope morphology The Journal of cell biology High 8682854
1995 Genetic interaction screens in yeast revealed that deletion of NUP188 alone is not lethal, but pairwise deletion combinations with POM152 or NUP170 are synthetically lethal, and NUP188 was identified as a major component comprising over one-fifth of the mass of the isolated yeast NPC together with Nup170p, Nup157p, Pom152p, and Nic96p. Synthetic lethal screen, direct microsequencing of NPC-enriched fractions, genetic complementation analysis The Journal of cell biology High 8522578
2000 Deletion of NUP188 (nup188-Δ) in yeast significantly increases passive nuclear envelope permeability: passive export rates of NLS-GFP reporters are faster, and equilibrium sieving limits for the NPC diffusion channel are larger than wild-type. This establishes Nup188p (together with Nup170p) as a determinant of the functional resting diameter of the NPC's central transport channel. In vivo fluorescence microscopy using NLS-GFP and NES-GFP reporters of varying sizes in nup188-Δ cells, passive diffusion measurements The Journal of cell biology High 10831607
1999 Elevated levels of Ssa1p (but not Ssb1p) suppress the NLS-GFP nuclear localization defects of nup188-Δ cells, placing Nup188p functionally upstream of Hsp70-assisted NLS-directed import. The differential suppression mapped to the nuclear export signal (NES) of Ssb1p, not to ATPase or peptide-binding domain differences, demonstrating a specific functional connection between Nup188p and cytosolic Hsp70 in nuclear transport. Genetic suppression analysis in nup188-Δ yeast, GFP reporter localization, chimeric Hsp70 constructs The Journal of biological chemistry Medium 10347213
1997 N-Nup145p (the GLFG-containing N-terminal cleavage product of Nup145p) becomes essential in a nup188 mutant background, demonstrating a synthetic lethal genetic interaction. Generation of the free N-domain by in vivo cleavage is required to complement this interaction, placing Nup188p in a functional network with GLFG-nucleoporins at the NPC. Synthetic lethality analysis in nup188 mutant background, domain complementation assays The EMBO journal Medium 9305650
2000 Vertebrate Nup188 was identified using an organelle trap assay in Xenopus egg extracts. Xenopus Nup188 exists in a stable complex with xNup93 and xNup205, does not bind WGA directly but associates indirectly via N-acetylglucosamine-modified nucleoporins, and can assemble into annulate lamellae (a cytoplasmic NPC mimic). Human NUP188 was also identified as an ortholog. Organelle trap assay (affinity selection on WGA-Sepharose + in vitro annulate lamellae assembly), co-immunoprecipitation, biotinylation tagging Molecular biology of the cell High 11029043
2013 Crystal structure of yeast Nup188 was determined, revealing an extended stack of helices where the N-terminal ~130 kDa segment forms an intricate closed ring and the C-terminal region is a superhelical structure with distant similarity to S-shaped nuclear transport receptors (NTRs). Both Nup188 and Nup192 specifically bind FG-repeats and can translocate through NPCs by facilitated diffusion, blurring the distinction between stationary scaffold nucleoporins and soluble NTRs. X-ray crystallography (structure determination), FG-repeat binding assays, in vivo NPC translocation assays eLife High 23795296
2013 Human Nup188 localizes to spindle poles during mitosis through its C-terminal region. Depletion of Nup188 causes failure of chromosome alignment at the metaphase plate, mitotic arrest via the spindle assembly checkpoint, and loss of robust K-fiber formation. Nup188 physically interacts with NuMA, and NuMA localization to spindle poles is perturbed in Nup188-depleted cells, establishing a mitotic function for Nup188 in chromosome segregation via K-fiber formation and NuMA recruitment. RNAi knockdown with live-cell imaging, immunofluorescence for spindle pole localization, co-immunoprecipitation (Nup188-NuMA interaction), spindle assembly checkpoint analysis Cancer science High 23551833
2016 Nup188 (together with Nup205) assists Nup93 in mediating repression of the HOXA gene cluster at the nuclear periphery. Depletion of the Nup93 sub-complex (Nup93/Nup188/Nup205) significantly upregulates HOXA gene expression, disengages the HOXA locus from the nuclear periphery (by 3D-FISH), increases active histone marks (H3K9ac), decreases repressive marks (H3K27me3), and increases transcription elongation marks (H3K36me3) on HOXA1. siRNA knockdown, ChIP, 3D-FISH, histone mark analysis by ChIP, RT-qPCR for gene expression Epigenetics & chromatin Medium 27980680
2017 GLFG repeats of Nup116 function redundantly with Nup188, a nonessential scaffold nucleoporin, to stabilize critical interactions within the NPC scaffold needed for late steps of NPC assembly. Direct in vitro binding between GLFG-containing FG repeats and multiple scaffold Nups including Nup188 was demonstrated, revealing a structural 'Velcro' role for natively unfolded FG repeats in linking NPC subcomplexes. In vitro binding assays (FG-repeat/scaffold interaction), genetic epistasis (nup116Δ nup188 double mutants), in vivo NPC assembly assays Cell High 29033133
2018 In budding yeast, Brl1 interacts with Nup188 by co-immunoprecipitation and with NPC components by split-YFP analysis. Brr6/Brl1 associate transiently with NPC assembly sites and promote NPC biogenesis; depletion causes NPC biogenesis defects while assembled NPCs remain intact, placing Nup188 within the Brl1-dependent NPC assembly pathway. Co-immunoprecipitation, split-YFP interaction analysis, conditional degron depletion, fluorescence microscopy of NPC assembly The Journal of cell biology Medium 29439116
2018 Quantitative fluorescence microscopy (NuRIM) revealed that Nup188 and its paralog Nup192 form a paralog pair whose altered expression leads to significant changes in NPC stoichiometry: overexpression of one leads to substitution for the other, revealing compositional plasticity at the NPC inner ring. Quantitative fluorescence microscopy (NuRIM), genetic manipulation of Nup188/Nup192 expression levels Proceedings of the National Academy of Sciences of the United States of America Medium 29632211
2019 TDP-43 controls mRNA splicing of NUP188; complete knockout of TDP-43 in human cells results in aberrant Nup188 mRNA splicing, and this is accompanied by nuclear envelope morphological defects, establishing TDP-43 as a trans-acting splicing regulator of NUP188. TDP-43 knockout cell lines, transcriptomic analysis, RT-PCR validation of splicing defects, cell biological analysis of nuclear envelope morphology Life science alliance Medium 31527135
2020 Nup188 populates centrosomes (pericentriolar material, PCM) with newly synthesized protein that does not exchange with NPCs even after mitotic NPC breakdown. The PCM pool is subject to proteasomal degradation while the NPC pool is not, establishing differential turnover as a mechanism segregating Nup188 between the two compartments. Nup188 directly binds Cep152 and functions in centriole duplication at or upstream of Sas6 loading, linking its centrosomal role to congenital heart disease mechanisms. Pulse-chase fluorescent labeling, proximity-labeling (BioID), super-resolution microscopy, proteasome inhibitor experiments, direct binding assay (Nup188-Cep152), Nup188 depletion with Sas6 loading assay The Journal of cell biology High 32211895
2022 Cryo-EM and crystal structures of intact Nup188 (and Nup192) scaffold hubs bound to linker nucleoporin binding regions (Nic96, Nup145N, Nup53) were determined, revealing Nup188 as a question mark-shaped keystone of two evolutionarily conserved hetero-octameric inner ring complexes. Linkers bind to scaffold surface pockets through short defined motifs. Quantitative docking into cryo-ET maps of constricted and dilated NPCs positioned Nup188 in the intact fungal and human NPC and revealed that the linker-scaffold network allows inner ring constriction/dilation while outer ring spokes are cross-link stapled and restricted from dilation. Single-particle cryo-EM, X-ray crystallography, biochemical reconstitution, cryo-ET docking, structure-guided mutagenesis in S. cerevisiae Science (New York, N.Y.) High 35679425
2022 NUP188 was identified as a Nesprin-2-interacting partner of the LINC complex at the nuclear envelope. Cytosol-localized SV40 polyomavirus is targeted to the nuclear envelope via Nesprin-2, which positions NUP188/NPC to capture the virus and facilitate nuclear translocation. This defines NUP188 as a physical bridge between the LINC complex and NPC for cargo handoff. Co-immunoprecipitation (Nesprin-2/NUP188 interaction), siRNA knockdown with viral infection assays, fluorescence microscopy tracking of SV40 nuclear entry PLoS pathogens Medium 36067270
2011 Morpholino knockdown of NUP188 in Xenopus strongly disrupts both morphological left-right (LR) development and expression of pitx2, a molecular marker of LR patterning, identifying NUP188 as a gene required for LR body patterning, likely through a cilia-related mechanism at the gastrocoel roof plate LR organizer. Morpholino knockdown in Xenopus, in situ hybridization for pitx2 expression, morphological scoring of LR defects Proceedings of the National Academy of Sciences of the United States of America Medium 21282601
2018 A cold-sensitive nup188-brr7 allele causes defects in select protein import pathways as well as mRNA export in S. cerevisiae, linking Nup188 function specifically to nucleocytoplasmic transport through the Nic96 nucleoporin complex. Genetic screen (cold-sensitive mRNA export), dT50 in situ hybridization for poly-A RNA export, protein import assays in nup188 mutant G3 (Bethesda, Md.) Medium 30021831
2025 A genome-wide screen in yeast identified Nup188 as required for break-induced replication (BIR) completion, acting later than Nup84. Nup188 functions after DNA synthesis to support BIR repair completion, placing it sequentially in the BIR pathway distinct from its NPC structural role. Genome-wide genetic screen for BIR deficiency, validation by epistasis analysis of nup188 deletion in BIR assay Nature communications Medium 41398407
1999 Full-length Pom152p (including its lumenal C-terminal domain) is required to rescue nup188 mutations, while the N-terminal domain alone can rescue nic96 and nup59 mutants, demonstrating that Nup188p's functional interaction with Pom152p requires the lumenal structures of Pom152p and implicating the pore membrane-to-scaffold connection in NUP188 function. Domain complementation assays of Pom152p in nup188 and other nup mutant backgrounds, topology mapping by alkaline extraction and protease protection The Journal of biological chemistry Medium 9988776

Source papers

Stage 0 corpus · 66 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2009 Defining the human deubiquitinating enzyme interaction landscape. Cell 1282 19615732
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
2018 VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near stop codon and associates with alternative polyadenylation. Cell discovery 829 29507755
2007 Large-scale mapping of human protein-protein interactions by mass spectrometry. Molecular systems biology 733 17353931
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2012 A census of human soluble protein complexes. Cell 689 22939629
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2018 High-Density Proximity Mapping Reveals the Subcellular Organization of mRNA-Associated Granules and Bodies. Molecular cell 580 29395067
2021 Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoV. Nature 532 33845483
2011 Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes and pathways. Cell 507 21565611
2014 Probing nuclear pore complex architecture with proximity-dependent biotinylation. Proceedings of the National Academy of Sciences of the United States of America 436 24927568
2022 OpenCell: Endogenous tagging for the cartography of human cellular organization. Science (New York, N.Y.) 432 35271311
2010 Systematic analysis of human protein complexes identifies chromosome segregation proteins. Science (New York, N.Y.) 421 20360068
2015 Panorama of ancient metazoan macromolecular complexes. Nature 407 26344197
2009 Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair. Cell 375 19596235
2021 A proximity-dependent biotinylation map of a human cell. Nature 339 34079125
2013 Integrated structural analysis of the human nuclear pore complex scaffold. Cell 284 24315095
2000 The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates. RNA (New York, N.Y.) 284 10668806
2012 A high-throughput approach for measuring temporal changes in the interactome. Nature methods 273 22863883
2004 Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. Nature biotechnology 266 15146197
2010 Identification and characterization of nuclear pore complex components in Arabidopsis thaliana. The Plant cell 239 21189294
2009 Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6. Science signaling 207 19738201
2011 Rare copy number variations in congenital heart disease patients identify unique genes in left-right patterning. Proceedings of the National Academy of Sciences of the United States of America 203 21282601
2018 An AP-MS- and BioID-compatible MAC-tag enables comprehensive mapping of protein interactions and subcellular localizations. Nature communications 201 29568061
2013 The protein interaction landscape of the human CMGC kinase group. Cell reports 174 23602568
1995 Two novel related yeast nucleoporins Nup170p and Nup157p: complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p. The Journal of cell biology 163 8522578
2019 H4K20me0 recognition by BRCA1-BARD1 directs homologous recombination to sister chromatids. Nature cell biology 162 30804502
2019 A protein-interaction network of interferon-stimulated genes extends the innate immune system landscape. Nature immunology 159 30833792
2016 Mutations in nuclear pore genes NUP93, NUP205 and XPO5 cause steroid-resistant nephrotic syndrome. Nature genetics 157 26878725
2007 Prominent use of distal 5' transcription start sites and discovery of a large number of additional exons in ENCODE regions. Genome research 154 17567994
2020 AMPK, a Regulator of Metabolism and Autophagy, Is Activated by Lysosomal Damage via a Novel Galectin-Directed Ubiquitin Signal Transduction System. Molecular cell 152 31995728
2022 Architecture of the linker-scaffold in the nuclear pore. Science (New York, N.Y.) 95 35679425
2000 Yeast nucleoporins involved in passive nuclear envelope permeability. The Journal of cell biology 94 10831607
1996 Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p. The Journal of cell biology 92 8682854
1997 Two functionally distinct domains generated by in vivo cleavage of Nup145p: a novel biogenesis pathway for nucleoporins. The EMBO journal 87 9305650
2017 Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex. Cell 83 29033133
1996 The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complex. The Journal of cell biology 78 8682855
2018 Stoichiometry and compositional plasticity of the yeast nuclear pore complex revealed by quantitative fluorescence microscopy. Proceedings of the National Academy of Sciences of the United States of America 59 29632211
2013 Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors. eLife 59 23795296
1999 A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. The Journal of biological chemistry 53 10347213
2000 Identification of a new vertebrate nucleoporin, Nup188, with the use of a novel organelle trap assay. Molecular biology of the cell 46 11029043
2019 Pleiotropic requirements for human TDP-43 in the regulation of cell and organelle homeostasis. Life science alliance 45 31527135
2013 Nucleoporin Nup188 is required for chromosome alignment in mitosis. Cancer science 45 23551833
2016 HOXA repression is mediated by nucleoporin Nup93 assisted by its interactors Nup188 and Nup205. Epigenetics & chromatin 44 27980680
2011 Traversing the NPC along the pore membrane: targeting of membrane proteins to the INM. Nucleus (Austin, Tex.) 41 21738830
2017 Whole Exome Sequencing Identifies Truncating Variants in Nuclear Envelope Genes in Patients With Cardiovascular Disease. Circulation. Cardiovascular genetics 35 28611029
2018 Brr6 and Brl1 locate to nuclear pore complex assembly sites to promote their biogenesis. The Journal of cell biology 34 29439116
1999 Topology and functional domains of the yeast pore membrane protein Pom152p. The Journal of biological chemistry 32 9988776
2008 Yeast screens identify the RNA polymerase II CTD and SPT5 as relevant targets of BRCA1 interaction. PloS one 29 18197258
2020 Biallelic loss of function NEK3 mutations deacetylate α-tubulin and downregulate NUP205 that predispose individuals to cilia-related abnormal cardiac left-right patterning. Cell death & disease 16 33230144
2019 NUP188 Biallelic Loss of Function May Underlie a New Syndrome: Nucleoporin 188 Insufficiency Syndrome? Molecular syndromology 16 32021605
2021 Proteomic Response of Rat Pituitary Under Chronic Mild Stress Reveals Insights Into Vulnerability and Resistance to Anxiety or Depression. Frontiers in genetics 15 34603401
2020 Differential turnover of Nup188 controls its levels at centrosomes and role in centriole duplication. The Journal of cell biology 14 32211895
2010 Recurrent deletion of 9q34 in adult normal karyotype precursor B-cell acute lymphoblastic leukemia. Cancer genetics and cytogenetics 12 20417863
2023 Non-classical functions of nuclear pore proteins in ciliopathy. Frontiers in molecular biosciences 7 37908226
2022 A Boy with Sandestig-Stefanova Syndrome and Genital Abnormalities. Molecular syndromology 6 36158057
2022 Components of the LINC and NPC complexes coordinately target and translocate a virus into the nucleus to promote infection. PLoS pathogens 5 36067270
2018 Identification of the Novel Nup188-brr7 Allele in a Screen for Cold-Sensitive mRNA Export Mutants in Saccharomyces cerevisiae. G3 (Bethesda, Md.) 5 30021831
2010 Small-interfering RNA-mediated silencing of the MAPK p42 gene induces dual effects in HeLa cells. Oncology letters 4 22966358
2025 Serum Proteomics Analysis of Patients with Ascending Aortic Dilation. Cardiovascular toxicology 2 40169515
2025 Genome-wide screen reveals dependence of break induced replication on several distinct checkpoints. Nature communications 2 41398407
2022 Gene network profiling in muscle-invasive bladder cancer: A systematic review and meta-analysis. Urologic oncology 2 35039218
2024 A Novel Truncating Variant in Sandestig-Stefanova Syndrome with Hydrocephalus. Molecular syndromology 1 39911172
2025 A Novel Homozygous Splice Variant in the NUP188 Gene Causing Sandestig-Stefanova Syndrome in a Saudi Patient. American journal of medical genetics. Part A 0 40859750