| 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; it was localized to the NPC by immunoelectron microscopy. |
Molecular cloning, sequencing, immunoelectron microscopy, biochemical fractionation |
The Journal of biological chemistry |
High |
8021268
|
| 1997 |
Human Nup84 (NUP107) is tightly associated with CAN/Nup214 on the cytoplasmic face of the NPC; the NH2-terminal region of Nup84 contains the interaction site with CAN/Nup214, while the C-terminal putative coiled-coil domain is required for association with the cytoplasmic face of the NPC. |
Immunoprecipitation under nondenaturing conditions, mutagenesis, expression studies, cytoplasmic face localization determination |
The Journal of cell biology |
High |
9166401
|
| 2003 |
Depletion of Nup107 by siRNA caused co-depletion of Nup133 (but not Nup96 or Sec13) and prevented assembly of Nup358, Nup214, Nup153, and Tpr into the NPC, establishing Nup107 as a keystone nucleoporin required for assembly of a subset of nucleoporins into the NPC. |
siRNA knockdown in HeLa cells, Western blot, RT-PCR, immunofluorescence |
Proceedings of the National Academy of Sciences of the United States of America |
High |
12552102
|
| 2004 |
The Nup107-160 complex in vertebrates includes three additional WD-repeat nucleoporins (Nup37, Nup43, and Seh1/Sec13), and the entire complex is targeted to kinetochores from prophase to anaphase of mitosis. |
Biochemical co-purification, GFP-tagged nucleoporin imaging, specific antibody immunofluorescence, RNAi |
Molecular biology of the cell |
High |
15146057
|
| 2004 |
The fission yeast Nup107-120 complex (ortholog of the vertebrate Nup107-160 complex) is required for mRNA export, nuclear pore distribution, and proper cell division; it functionally interacts with the small GTPase Ran/Spi1, as overexpression of a nonfunctional Ran allele is specifically toxic in nup120 and nup133b deletion mutants. |
Gene deletion, biochemical co-purification, nuclear envelope localization, genetic epistasis/synthetic lethality, mRNA export assay |
Molecular and cellular biology |
High |
15226438
|
| 2005 |
The yeast Nup84 subcomplex mediates Rap1/Gcr1/Gcr2 transcriptional activation ('reverse recruitment'); Nup84 and associated subcomplex components can activate transcription themselves when fused to a heterologous DNA-binding domain, and Gcr1/Gcr2 bridge the NPC to the transcriptional machinery. |
In vivo transcriptional activation assay with heterologous DNA-binding domain fusions, genetic analysis |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
15817685
|
| 2007 |
The Nup107-160 complex interacts with CENP-F and its kinetochore recruitment mainly depends on the Ndc80 complex; depletion of the Nup107-160 complex from kinetochores causes mitotic delay, impaired chromosome congression, reduced kinetochore tension, and kinetochore-microtubule attachment defects; the Nup107-160 complex at kinetochores is required for recruitment of Crm1 and RanGAP1-RanBP2 to kinetochores. |
Co-immunoprecipitation, siRNA depletion, immunofluorescence, live-cell imaging, kinetochore tension measurement |
The EMBO journal |
High |
17363900
|
| 2007 |
Nup107, Nup96, Nup133, and Nup160 subunits of the Nup107-160 complex are phosphorylated in a cell-cycle-dependent manner; phosphorylation sites cluster at the N-terminal disordered regions; the Nup107-160 subcomplex remains stable throughout the cell cycle, indicating phosphorylation regulates its association with the NPC rather than intra-complex interactions. |
In vivo 32P labeling, multi-stage mass spectrometry (MS/MS2/MS3), stable isotope labeling, cell-cycle synchronization |
Proceedings of the National Academy of Sciences of the United States of America |
High |
17360435
|
| 2008 |
Crystal structure of the Nup107-Nup133 heterodimer reveals elongated structures interacting via a compact interface in tail-to-tail fashion; structure-guided mutagenesis shows Nup107 is the critical anchor for Nup133 to the NPC, positioning Nup133 at the NPC periphery. |
X-ray crystallography, structure-guided mutagenesis, NPC assembly assays |
Molecular cell |
High |
18570875
|
| 2009 |
The Nup84-Nup145C-Sec13 heterotrimer forms the edge element of the NPC Y-complex lattice; the ACE1 heterotypic interaction between Nup84 and Nup145C is analogous to the homotypic ACE1 interaction of Sec31 in COPII lattice, supporting a lattice model for NPC scaffold architecture. |
X-ray crystallography of the 134-kDa heterotrimeric complex |
Nature structural & molecular biology |
High |
19855394
|
| 2009 |
Seh1, a component of the Nup107-160 complex, regulates centromeric localization of Aurora B and other chromosome passenger complex (CPC) proteins; Seh1 depletion causes impaired Aurora B localization, biorientation defects, and spindle midzone/midbody organization defects, while microtubule-kinetochore attachments remain intact. |
siRNA depletion, immunofluorescence, electron microscopy, live-cell imaging |
Molecular biology of the cell |
Medium |
19864462
|
| 2010 |
Depletion of Nup107 by siRNA in senescent human diploid fibroblasts prevents effective nuclear translocation of phosphorylated ERK following EGF stimulation and decreases c-Fos expression, implicating Nup107 in nuclear trafficking of signal molecules. |
siRNA knockdown, immunofluorescence for phospho-ERK, Western blot for c-Fos |
Biochemical and biophysical research communications |
Medium |
20833136
|
| 2011 |
SENP2 interacts with the Nup107-160 nucleoporin subcomplex through a distinct N-terminal targeting element; disruption of this interaction (along with karyopherin-mediated tethering) enhances SENP2 substrate accessibility, suggesting NPC-tethering regulates SUMO pathway activity. |
FRAP, Co-IP/pulldown, deletion/mutant constructs, NPC localization assays in human cells |
Molecular biology of the cell |
Medium |
22031293
|
| 2011 |
The yeast Nup84 complex is required for efficient transcription elongation, as demonstrated by a G-less-based run-on assay and RNA polymerase II chromatin immunoprecipitation. |
G-less-based run-on (GLRO) assay, RNA polymerase II ChIP, mutant analysis |
The EMBO journal |
Medium |
21478823
|
| 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; NUP107 physically and genetically interacts with spindle assembly checkpoint protein MAD1/MDF-1, and is required for MAD1's nuclear envelope accumulation. |
Genetic disruption (null mutant), immunofluorescence, Co-immunoprecipitation, genetic epistasis, nuclear protein import assay |
Molecular biology of the cell |
High |
22238360
|
| 2013 |
Reconstituted octameric Nup84 complex from Chaetomium thermophilum (carrying Nup37 and Elys) forms a dimer with side-to-side arrangement; crosslinking mass spectrometry mapped key protein interfaces within the Y-complex; Elys binds cooperatively requiring both Nup37 and Nup120. |
Protein reconstitution, electron microscopy, crosslinking mass spectrometry |
Structure (London, England : 1993) |
High |
23954503
|
| 2015 |
Nup153 recruits the Nup107-160 complex to assembly sites at the inner nuclear membrane for interphasic (but not mitotic exit) NPC assembly; Nup153 binds directly to the inner nuclear membrane via an N-terminal amphipathic helix, and transportin and Ran regulate this membrane interaction. |
siRNA depletion, immunofluorescence, in vitro membrane binding assay, mutational analysis |
Developmental cell |
High |
26051542
|
| 2015 |
Three of four NUP107 disease mutations detected in patients with steroid-resistant nephrotic syndrome impair NUP107 binding to NUP133 and NUP107 incorporation into NPCs in vitro, establishing that loss of NUP107–NUP133 interaction is a molecular mechanism underlying the disease. |
In vitro binding assay, NPC incorporation assay with mutant proteins, zebrafish morpholino knockdown |
American journal of human genetics |
Medium |
26411495
|
| 2015 |
A fraction of Nup107 (as part of the Y-complex) localizes within intranuclear GLFG bodies along with Nup98 and Elys; this intranuclear pool of the Y-complex is dynamically mobile (shown by FRAP), unlike the stable NPC-associated pool; Y-complex recruitment into GLFG bodies requires the C-terminal domain of Nup98. |
Immunofluorescence, co-localization, FRAP, GFP-tagging, siRNA depletion |
Molecular biology of the cell |
Medium |
25904327
|
| 2015 |
Nup107 directly binds Apaf-1 via the CED-4 domain of Apaf-1 and the central domain of Nup107 in an ATR-regulated, phosphorylation-dependent manner; this interaction is required for Apaf-1 nuclear import upon DNA damage, which in turn is required for Chk-1 activation and intra-S phase checkpoint. |
Co-immunoprecipitation, direct binding assay, dominant-negative interference, siRNA, cell cycle checkpoint assay |
Cell cycle (Georgetown, Tex.) |
Medium |
25695197
|
| 2019 |
In fission yeast, the Nup107-160 complex components show asymmetrical localization: spNup132 and spNup107 localize only to the nuclear side, while spNup131, spNup120, spNup85, spNup96, spNup37, spEly5, and spSeh1 localize only to the cytoplasmic side; fusion of spNup96 with spNup107 caused cytoplasmic mislocalization of spNup107 and led to cell cycle defects similar to spNup132 deletion. |
Immunoelectron microscopy, fluorescence microscopy, domain-fusion experiments, cell cycle analysis |
PLoS genetics |
High |
31170156
|
| 2019 |
The yeast Nup84 complex is required for efficient nucleotide excision repair (NER) of UV-induced lesions, repair of replication-born DSBs by sister chromatid recombination (SCR), and prevention of chromosomal rearrangements; nup84Δ cells show exacerbated UV sensitivity in S phase and delayed replication fork progression. |
UV sensitivity assays, NER assays, sister chromatid recombination assays, replication fork progression analysis |
Nucleic acids research |
Medium |
30715474
|
| 2020 |
Crystal structures of the full-length yeast Nup84-Nup133CTD complex and the Nup133NTD (bound to nanobodies) reveal high flexibility of this dimeric unit; the Nup133 NTD contains a structurally conserved amphipathic lipid packing sensor (ALPS) motif confirmed by liposome interaction studies. |
X-ray crystallography (nanobody-bound structures), liposome interaction assay |
Nature communications |
High |
33247142
|
| 2025 |
In C9orf72-ALS motor neurons, G3BP1 (a core stress granule component) exhibits enhanced interaction with Nup107, and Nup107 colocalizes with and aggregates in stress granules; knockdown of the C. elegans Nup107 ortholog (npp-5) alleviates ALS-associated phenotypes including reduced lifespan and impaired motility. |
Co-immunoprecipitation in iPSC-derived motor neurons, immunofluorescence co-localization, C. elegans npp-5 RNAi knockdown with lifespan/motility assays |
FEBS letters |
Medium |
40891053
|
| 2025 |
In Xenopus, Nup107 is required to prevent premature nuclear export of pri-miR427 before processing; depletion of Nup107 leads to reduced mature miR427 production, stabilization of maternal transcripts including REST, and disruption of the maternal-to-zygotic transition with expansion of ectoderm at the expense of endoderm and mesoderm. |
Morpholino depletion in Xenopus embryos, RNA-sequencing time course, nuclear/cytoplasmic fractionation, miRNA quantification, in situ hybridization |
Development (Cambridge, England) |
Medium |
39791357
|
| 2026 |
In Drosophila, Nup107 is required for nuclear translocation and transcriptional activation by the ecdysone receptor (EcR) and for transcription of Halloween genes (ecdysone biosynthesis genes); Nup107 functions epistatically downstream of the Torso receptor tyrosine kinase/Ras/MAPK pathway to activate EcR signaling during metamorphosis. |
RNAi knockdown, genetic epistasis (overexpression of torso/ras in Nup107-depleted background), EcR nuclear localization assay, gene expression analysis |
eLife |
Medium |
41805630
|