Affinage

NUP107

Nuclear pore complex protein Nup107 · UniProt P57740

Length
925 aa
Mass
106.4 kDa
Annotated
2026-04-29
40 papers in source corpus 18 papers cited in narrative 18 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NUP107 is a structural scaffold nucleoporin of the conserved Nup107-160 (Y-complex) that is essential for nuclear pore complex assembly, selective nucleocytoplasmic transport, and mitotic chromosome segregation. Its C-terminal domain forms a direct tail-to-tail interaction with NUP133 that anchors NUP133 at the NPC periphery, and depletion of NUP107 prevents incorporation of NUP133, NUP358, NUP214, NUP153, and Tpr into nuclear pores while also impairing mRNA export and nuclear import of specific cargoes including phospho-ERK and Apaf-1 (PMID:18570875, PMID:12552102, PMID:20833136, PMID:25695197). During mitosis, the Nup107-160 complex is recruited to kinetochores via the Ndc80 complex, where it promotes Aurora B/CPC localization, chromosome congression, spindle checkpoint signaling through interaction with MAD1, and recruitment of CRM1 and RanGAP1-RanBP2 (PMID:17363900, PMID:22238360, PMID:19864462). Biallelic NUP107 mutations that disrupt the NUP107–NUP133 interaction cause steroid-resistant nephrotic syndrome with podocyte foot process effacement (PMID:26411495).

Mechanistic history

Synthesis pass · year-by-year structured walk · 10 steps
  1. 1994 High

    Establishing NUP107 as a structural (non-FG-repeat) nucleoporin with kinase consensus sites answered the question of whether this protein belongs to the scaffold or transport-interface class of NPC components.

    Evidence Molecular cloning, sequencing, and immuno-EM of isolated nuclear envelope fractions

    PMID:8021268

    Open questions at the time
    • No functional data on what NUP107 does within the NPC
    • Kinase sites identified but not mapped to specific kinases or cell-cycle phases
  2. 2003 High

    Demonstrating that NUP107 depletion causes co-loss of NUP133 and prevents assembly of NUP358, NUP214, NUP153, and Tpr into NPCs established NUP107 as a keystone nucleoporin with hierarchical assembly functions.

    Evidence siRNA depletion in HeLa cells with immunofluorescence and western blotting of multiple nucleoporins

    PMID:12552102

    Open questions at the time
    • Mechanism by which NUP107 loss prevents downstream nucleoporin assembly was unclear
    • Whether NUP107 acts as a direct binding platform or indirectly through complex integrity was not resolved
  3. 2004 High

    Discovery that the entire Nup107-160 complex relocates to kinetochores during mitosis, combined with fission yeast genetic data linking the orthologous complex to mRNA export and the Ran pathway, expanded NUP107's role beyond interphase NPC function to mitotic regulation and RNA export.

    Evidence GFP tagging, RNAi, and live-cell imaging in human cells; genetic deletion and epistasis with Ran pathway in S. pombe

    PMID:15146057 PMID:15226438

    Open questions at the time
    • Mechanism of kinetochore recruitment unknown
    • Which mitotic functions depend on Y-complex versus individual subunits was unresolved
  4. 2007 High

    Identification of the Ndc80 complex as the primary kinetochore receptor for the Nup107-160 complex, together with comprehensive mitotic phosphorylation mapping of NUP107, resolved how the Y-complex reaches kinetochores and how its NPC association is cell-cycle-regulated.

    Evidence Reciprocal Co-IP, multiple siRNA conditions, live-cell imaging for kinetochore recruitment; SILAC-based quantitative phosphoproteomics with cell-cycle staging

    PMID:17360435 PMID:17363900

    Open questions at the time
    • Functional consequences of individual phosphorylation sites untested
    • Whether phosphorylation directly controls NPC dissociation or kinetochore binding was not distinguished
  5. 2008 High

    Crystal structure of the NUP107–NUP133 C-terminal domain complex, showing a tail-to-tail architecture, answered how NUP107 anchors NUP133 at the NPC periphery and provided a structural basis for disease mutations.

    Evidence X-ray crystallography of recombinant human NUP107–NUP133 complex with structure-guided mutagenesis

    PMID:18570875

    Open questions at the time
    • Full-length Y-complex architecture not resolved
    • Whether the NUP107–NUP133 interface is regulated post-translationally was not addressed
  6. 2009 High

    Showing that the Y-complex subunit Seh1 controls Aurora B/CPC localization at centromeres connected the kinetochore-localized Y-complex to the error correction machinery for chromosome biorientation.

    Evidence Seh1 siRNA depletion with immunofluorescence, EM, and live-cell imaging

    PMID:19864462

    Open questions at the time
    • Whether NUP107 itself is the CPC-recruiting subunit or acts indirectly through Seh1 was unclear
    • Mechanism of CPC recruitment by Y-complex components not defined
  7. 2010 Medium

    Demonstrating that NUP107 is required for nuclear translocation of phospho-ERK after EGF stimulation established a specific cargo-selective transport function for NUP107 in growth factor signaling.

    Evidence siRNA knockdown in human diploid fibroblasts with subcellular fractionation and western blotting

    PMID:20833136

    Open questions at the time
    • Whether NUP107 directly binds phospho-ERK or acts indirectly through NPC structural integrity not determined
    • Single cell type and single lab study
  8. 2012 High

    Genetic studies in C. elegans and zebrafish established that NUP107 physically interacts with MAD1 for spindle checkpoint signaling, controls Aurora B levels at kinetochores, and is required in vivo for tissue-specific NPC integrity, mRNA export, and cell survival.

    Evidence C. elegans mutant analysis with Co-IP and genetic epistasis; zebrafish insertional mutagenesis with immunofluorescence and mRNA export assays

    PMID:22238360 PMID:22965233

    Open questions at the time
    • Whether tissue-specific phenotypes in zebrafish reflect differential NUP107 dependence versus differential sensitivity to NPC loss
    • Direct versus indirect nature of MAD1 interaction with NUP107 at molecular level
  9. 2015 High

    Four parallel advances resolved how NUP107 reaches interphase NPCs (via Nup153-mediated inner nuclear membrane recruitment), how its mutation causes human disease (biallelic mutations disrupting NUP133 binding cause nephrotic syndrome with podocyte defects), and defined a novel cargo-specific transport function (ATR-phosphorylation-dependent Apaf-1 nuclear import through direct NUP107 binding).

    Evidence Direct binding assays and mutagenesis of Nup153; in vitro binding of NUP107 disease mutants and zebrafish morpholino knockdown with podocyte EM; Co-IP and domain mapping for Apaf-1–NUP107 interaction

    PMID:25695197 PMID:26051542 PMID:26411495

    Open questions at the time
    • Whether Nup153-mediated recruitment is the sole interphase pathway for Y-complex insertion
    • Molecular mechanism linking NUP107 loss specifically to podocyte failure versus general NPC dysfunction
    • Apaf-1 import mechanism based on single-lab Co-IP and dominant-negative approach
  10. 2025 Medium

    Recent work revealed NUP107 mislocalization into stress granules in C9-ALS motor neurons and a developmental role in nuclear retention and processing of pri-miRNAs required for the maternal-to-zygotic transition.

    Evidence Co-IP from iPSC-derived motor neurons with C. elegans genetic rescue; morpholino depletion in Xenopus with RNA-seq time course and epistasis

    PMID:39791357 PMID:40891053

    Open questions at the time
    • Whether NUP107 stress-granule sequestration is causal for ALS pathology or a secondary consequence
    • Whether pri-miRNA retention function is a general NPC property or specific to NUP107/Y-complex
    • Neither finding independently replicated

Open questions

Synthesis pass · forward-looking unresolved questions
  • Open questions include the precise structural mechanism by which the Y-complex recruits CPC/Aurora B to kinetochores, how individual NUP107 phosphorylation events regulate its partitioning between NPCs and kinetochores, and whether NUP107's cargo-selective transport roles (phospho-ERK, Apaf-1, pri-miRNA retention) reflect direct NUP107-cargo contacts or indirect effects of Y-complex-dependent NPC architecture.
  • No reconstituted system for Y-complex–CPC interaction
  • Phosphosite mutant analysis in mammalian cells lacking
  • Structural basis for cargo selectivity through NUP107 unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 4
Localization
GO:0005635 nuclear envelope 4 GO:0005694 chromosome 4 GO:0005634 nucleus 2
Pathway
R-HSA-1640170 Cell Cycle 5 R-HSA-8953854 Metabolism of RNA 3 R-HSA-9609507 Protein localization 3
Partners
APAF1G3BP1MAD1NDC80NUP133NUP153NUP96SEH1L
Complex memberships
Nuclear pore complexNup107-160 complex (Y-complex)

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1994 NUP107 was identified as a novel nuclear pore complex protein containing a leucine zipper in its carboxyl-terminal region and numerous kinase consensus sites, but lacking FG repeats, establishing it as a structural nucleoporin component. Molecular cloning, sequencing, and immunoelectron microscopy of isolated nuclear envelope proteins The Journal of biological chemistry High 8021268
2003 NUP107 functions as a keystone nucleoporin required for the assembly of a subset of other nucleoporins into the NPC; depletion of Nup107 caused co-depletion of Nup133 protein and prevented assembly of Nup358, Nup214, Nup153, and Tpr into NPCs, while Nup96, Sec13, and p62 were unaffected. siRNA depletion of Nup107 in HeLa cells followed by immunofluorescence and western blotting of other nucleoporins Proceedings of the National Academy of Sciences of the United States of America High 12552102
2004 The entire Nup107-160 complex, including three newly identified members Nup37, Nup43, and Seh1, is recruited as a complete entity to kinetochores from prophase to anaphase during mitosis. GFP-tagged nucleoporins, RNAi depletion, specific antibodies, and live-cell fluorescence microscopy Molecular biology of the cell High 15146057
2004 The fission yeast Nup107-120 complex (ortholog of human Nup107-160) is required for mRNA export, nuclear pore distribution, and proper cell division; deletion mutants show cell division defects resembling Ran GTPase cycle mutants, and a functional/genetic link to the Ran/Spi1 pathway was established. Genetic deletion, biochemical fractionation, fluorescence microscopy, and genetic epistasis with Ran pathway mutants in S. pombe Molecular and cellular biology High 15226438
2007 The Nup107-160 complex is recruited to kinetochores mainly through the Ndc80 complex, interacts with CENP-F (which contributes only moderately to kinetochore targeting), and its presence at kinetochores is required for the recruitment of Crm1 and RanGAP1-RanBP2 to kinetochores. Depletion causes mitotic delay, impaired chromosome congression, reduced kinetochore tension, and kinetochore-microtubule attachment defects. siRNA depletion of multiple subunits, co-immunoprecipitation, immunofluorescence, live-cell imaging The EMBO journal High 17363900
2007 Nup107, Nup96, Nup133, and Nup160 are phosphorylated in a cell-cycle-dependent manner, with phosphorylation sites clustered at N-terminal disordered regions and several events being specifically mitotic; phosphorylation does not disrupt intra-subcomplex interactions but likely regulates association of the Nup107-160 complex with the NPC and other proteins. In vivo 32P labeling, stable isotope labeling (SILAC), multi-stage mass spectrometry (MS/MS2/MS3), site-specific phosphorylation mapping Proceedings of the National Academy of Sciences of the United States of America High 17360435
2008 Crystal structure of human Nup107 C-terminal domain in complex with Nup133 C-terminal domain revealed that both proteins form elongated structures interacting via a compact interface in tail-to-tail fashion; structure-guided mutagenesis showed Nup107 is the critical anchor for Nup133 to the NPC, positioning Nup133 at the NPC periphery. X-ray crystallography of recombinant Nup107-Nup133 complex combined with structure-guided mutagenesis Molecular cell High 18570875
2009 Seh1, a component of the Nup107-160 complex, regulates chromosome alignment and segregation by controlling the centromeric localization of Aurora B and other chromosome passenger complex (CPC) proteins; microtubule-kinetochore attachments remain intact upon Seh1 depletion, but Aurora B mislocalization leads to biorientation defects and spindle midzone/midbody disorganization. Seh1 siRNA depletion, immunofluorescence, electron microscopy, live-cell imaging Molecular biology of the cell High 19864462
2011 SENP2 (SUMO-specific isopeptidase) is tethered to nuclear pore complexes partly through direct interaction with the Nup107-160 subcomplex via a dedicated targeting element in its N-terminus; disruption of this interaction enhances SENP2 substrate accessibility, implicating this tethering in SUMO pathway regulation. FRAP, Co-immunoprecipitation, deletion mutagenesis of SENP2 targeting elements Molecular biology of the cell Medium 22031293
2012 In C. elegans, NUP107/NPP-5 is essential for proper kinetochore localization of NUP133/NPP-15 but not NUP96/NPP-10C or ELYS/MEL-28; NPP-5 depletion reduces kinetochore NUF2/HIM-10 and Aurora B/AIR-2 kinase levels on mitotic chromatin; NPP-5 physically and genetically interacts with spindle assembly checkpoint protein MAD1/MDF-1 and is required for MAD1's nuclear envelope accumulation. Genetic disruption (C. elegans mutants), co-immunoprecipitation, immunofluorescence, genetic epistasis Molecular biology of the cell High 22238360
2015 Nup153 recruits the Nup107-160 complex to the inner nuclear membrane for NPC assembly specifically during interphase (not at mitotic exit); Nup153 binds directly to the inner nuclear membrane via an N-terminal amphipathic helix, and this binding facilitates Nup107-160 recruitment to assembly sites; transportin and Ran GTPase regulate this Nup153-membrane interaction. siRNA depletion, direct binding assays, mutagenesis of Nup153 amphipathic helix, cell fractionation, fluorescence microscopy Developmental cell High 26051542
2015 Biallelic NUP107 mutations disrupt binding of NUP107 to NUP133 and prevent NUP107 incorporation into NPCs in vitro; zebrafish nup107 morphants display hypoplastic glomerular structures and abnormal podocyte foot processes, establishing a role for NUP107 in podocyte function. In vitro binding assays with disease-associated mutants, zebrafish morpholino knockdown, electron microscopy of podocyte morphology American journal of human genetics High 26411495
2015 A fraction of the Nup107-160 complex (Y-complex) localizes dynamically within intranuclear GLFG bodies, colocalizing with Nup98; this intranuclear localization requires the C-terminal domain of Nup98, and FRAP studies show the Y-complex shuttles into and out of GLFG bodies more dynamically than at nuclear pores. GFP tagging, fluorescence microscopy, FRAP, Nup98 C-terminal domain deletion analysis Molecular biology of the cell Medium 25904327
2015 Apaf-1 associates with NUP107 and this association is required for Apaf-1 nuclear import upon DNA damage; the CED-4 domain of Apaf-1 directly binds the central domain of NUP107 in an ATR-regulated, phosphorylation-dependent manner; expression of the Apaf-1-interacting domain of NUP107 interfered with Apaf-1 nuclear translocation and reduced Chk-1 activation and cell cycle arrest. Co-immunoprecipitation, domain mapping, dominant-negative overexpression, cell cycle assays Cell cycle Medium 25695197
2010 Nup107 depletion by siRNA in young human diploid fibroblasts prevents nuclear translocation of phosphorylated ERK following EGF stimulation and decreases c-Fos expression, placing Nup107 as required for nuclear import of activated ERK in growth factor signaling. siRNA knockdown, subcellular fractionation/immunofluorescence of phospho-ERK, western blotting for c-Fos Biochemical and biophysical research communications Medium 20833136
2025 In C9-ALS motor neurons derived from patient iPSCs, G3BP1 (a core stress granule component) shows enhanced interaction with NUP107, and NUP107 colocalizes with and aggregates into stress granules; knockdown of the C. elegans NUP107 ortholog npp-5 alleviates ALS-associated phenotypes including reduced lifespan and impaired motility. Co-immunoprecipitation from iPSC-derived motor neurons, immunofluorescence colocalization, C. elegans genetic knockdown with behavioral phenotype assays FEBS letters Medium 40891053
2025 In Xenopus, Nup107 is required for nuclear retention and processing of pri-miR427 transcripts; depletion of Nup107 leads to premature nuclear export of pri-miR427, reduced mature miR427 production, stabilization of maternal transcripts, and failure of maternal-to-zygotic transition with germ layer patterning defects. Morpholino depletion in Xenopus, RNA-sequencing time course, functional epistasis with miR427 targets including REST Development Medium 39791357
2012 Loss of zygotic nup107 in zebrafish results in tissue-specific defects (loss of pharyngeal skeletons, intestine degeneration, absence of swim bladder, smaller eyes) with extensive apoptosis; affected tissues show disturbed FG-repeat nucleoporins, reduced nuclear pore number, and impaired mRNA nuclear export. Tol2 transposon insertional mutagenesis in zebrafish, immunofluorescence, in situ hybridization, mRNA export assays The Journal of biological chemistry Medium 22965233

Source papers

Stage 0 corpus · 40 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis. Molecular biology of the cell 223 15146057
2007 The human Nup107-160 nuclear pore subcomplex contributes to proper kinetochore functions. The EMBO journal 171 17363900
2003 Depletion of a single nucleoporin, Nup107, prevents the assembly of a subset of nucleoporins into the nuclear pore complex. Proceedings of the National Academy of Sciences of the United States of America 129 12552102
2015 Nup153 Recruits the Nup107-160 Complex to the Inner Nuclear Membrane for Interphasic Nuclear Pore Complex Assembly. Developmental cell 115 26051542
2005 Reverse recruitment: the Nup84 nuclear pore subcomplex mediates Rap1/Gcr1/Gcr2 transcriptional activation. Proceedings of the National Academy of Sciences of the United States of America 114 15817685
2015 Biallelic Mutations in Nuclear Pore Complex Subunit NUP107 Cause Early-Childhood-Onset Steroid-Resistant Nephrotic Syndrome. American journal of human genetics 99 26411495
1997 Nup84, a novel nucleoporin that is associated with CAN/Nup214 on the cytoplasmic face of the nuclear pore complex. The Journal of cell biology 88 9166401
2008 Structural and functional studies of Nup107/Nup133 interaction and its implications for the architecture of the nuclear pore complex. Molecular cell 84 18570875
2007 Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160 subcomplex. Proceedings of the National Academy of Sciences of the United States of America 83 17360435
2017 Homozygous mutation in NUP107 leads to microcephaly with steroid-resistant nephrotic condition similar to Galloway-Mowat syndrome. Journal of medical genetics 71 28280135
2012 Putative members of the Arabidopsis Nup107-160 nuclear pore sub-complex contribute to pathogen defense. The Plant journal : for cell and molecular biology 70 22288649
2004 The fission yeast Nup107-120 complex functionally interacts with the small GTPase Ran/Spi1 and is required for mRNA export, nuclear pore distribution, and proper cell division. Molecular and cellular biology 70 15226438
2009 The Nup107-160 nucleoporin complex promotes mitotic events via control of the localization state of the chromosome passenger complex. Molecular biology of the cell 69 19864462
2009 Molecular architecture of the Nup84-Nup145C-Sec13 edge element in the nuclear pore complex lattice. Nature structural & molecular biology 65 19855394
2011 The SUMO-specific isopeptidase SENP2 associates dynamically with nuclear pore complexes through interactions with karyopherins and the Nup107-160 nucleoporin subcomplex. Molecular biology of the cell 51 22031293
2011 A novel assay identifies transcript elongation roles for the Nup84 complex and RNA processing factors. The EMBO journal 49 21478823
2012 Dissection of the NUP107 nuclear pore subcomplex reveals a novel interaction with spindle assembly checkpoint protein MAD1 in Caenorhabditis elegans. Molecular biology of the cell 45 22238360
2013 Protein interfaces of the conserved Nup84 complex from Chaetomium thermophilum shown by crosslinking mass spectrometry and electron microscopy. Structure (London, England : 1993) 42 23954503
2015 Intranuclear dynamics of the Nup107-160 complex. Molecular biology of the cell 36 25904327
1994 Nup107 is a novel nuclear pore complex protein that contains a leucine zipper. The Journal of biological chemistry 35 8021268
2020 Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif. Nature communications 33 33247142
2017 NUP107 mutations in children with steroid-resistant nephrotic syndrome. Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association 29 27190346
2019 Asymmetrical localization of Nup107-160 subcomplex components within the nuclear pore complex in fission yeast. PLoS genetics 26 31170156
2012 Dissecting the NUP107 complex: multiple components and even more functions. Nucleus (Austin, Tex.) 26 22713280
2015 DNA damage-induced nuclear translocation of Apaf-1 is mediated by nucleoporin Nup107. Cell cycle (Georgetown, Tex.) 25 25695197
2012 Loss of zygotic NUP107 protein causes missing of pharyngeal skeleton and other tissue defects with impaired nuclear pore function in zebrafish embryos. The Journal of biological chemistry 23 22965233
2019 The Nup84 complex coordinates the DNA damage response to warrant genome integrity. Nucleic acids research 20 30715474
2018 Functional study of a novel missense single-nucleotide variant of NUP107 in two daughters of Mexican origin with premature ovarian insufficiency. Molecular genetics & genomic medicine 20 29363275
2010 Reduction of Nup107 attenuates the growth factor signaling in the senescent cells. Biochemical and biophysical research communications 16 20833136
2014 Analysis of the Lotus japonicus nuclear pore NUP107-160 subcomplex reveals pronounced structural plasticity and functional redundancy. Frontiers in plant science 13 24478780
2010 Characterization of the membrane-coating Nup84 complex: paradigm for the nuclear pore complex structure. Nucleus (Austin, Tex.) 11 21326946
2010 Depletion of a single nucleoporin, Nup107, induces apoptosis in eukaryotic cells. Molecular and cellular biochemistry 10 20490895
2001 Disruption and functional analysis of six ORFs of chromosome IV: YDL103c (QRI1), YDL105w (QRI2), YDL112w (TRM3), YDL113c, YDL116w (NUP84) and YDL167c (NRP1). Yeast (Chichester, England) 9 11180460
2024 Mutations in the NUP93, NUP107 and NUP160 genes cause steroid-resistant nephrotic syndrome in Chinese children. Italian journal of pediatrics 6 38650033
2007 Purification, crystallization and preliminary X-ray analysis of a Nup107-Nup133 heterodimeric nucleoporin complex. Acta crystallographica. Section F, Structural biology and crystallization communications 6 17768364
2020 Nup84 persists within the nuclear envelope of the rice blast fungus, Magnaporthe oryzae, during mitosis. Fungal genetics and biology : FG & B 3 32980454
2025 Nup107 contributes to the maternal-to-zygotic transition by preventing the premature nuclear export of pri-miR427. Development (Cambridge, England) 2 39791357
2025 C9orf72 ALS-causing mutations lead to mislocalization and aggregation of nucleoporin Nup107 into stress granules. FEBS letters 2 40891053
2026 Nup107 is a crucial regulator of torso-mediated metamorphic transition in Drosophila melanogaster. eLife 0 41805630
2024 Recurrent Increased Nuchal Translucency Led to the Identification of Novel NUP107 Variants. American journal of medical genetics. Part A 0 39473271