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Showing NOLC1 — NOPP140 is a alias.

NOLC1

Nucleolar and coiled-body phosphoprotein 1 · UniProt Q14978

Length
699 aa
Mass
73.6 kDa
Annotated
2026-06-10
56 papers in source corpus 26 papers cited in narrative 27 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/8 claims corpus-supported (88%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NOLC1/Nopp140 is a heavily phosphorylated, intrinsically disordered nucleolar phosphoprotein that shuttles between the nucleolus and cytoplasm along defined tracks extending from the dense fibrillar component to nuclear pores, and serves as a chaperone organizing ribosome biogenesis and Cajal body (CB) biology (PMID:1623516, PMID:29382046). Its extreme phosphorylation is executed by casein kinase II (CK2) at numerous serines, and the relationship is reciprocal: Nopp140 binds the CK2 regulatory beta subunit and the catalytic CK2alpha subunit with nanomolar affinity, inhibiting CK2 activity at the substrate-recognition site in a manner relieved by IP6, while CK2 binding rigidifies its disordered C-terminus (PMID:8702624, PMID:9013635, PMID:18790693, PMID:24218616, PMID:29382046). Through an alternating charged repeat domain, Nopp140 targets both the nucleolus and CBs and physically links the two compartments via coilin; multivalent coilin-NTD/Nopp140 contacts drive the biomolecular condensation that assembles CBs (PMID:9679133, PMID:36224177). In the nucleolus it associates with RNA polymerase I (RPA194) to support rDNA transcription, and concentrates IDR-rich factors to scaffold the dense fibrillar component as a phase-separated condensate ensuring efficient rRNA 2'-O-methylation (PMID:10567578). Nopp140 reversibly associates with both box H/ACA and box C/D snoRNPs without being required for their catalytic pseudouridylation activity, consistent with a chaperoning rather than enzymatic role; its loss redistributes fibrillarin, reduces rRNA modification, and collapses ribosome production and translation (PMID:10679015, PMID:12446766, PMID:25384888). It additionally recruits and retains all scaRNPs in CBs in a CK2-phosphorylation-dependent manner, thereby enabling snRNA 2'-O-methylation that safeguards splicing fidelity, and controls telomerase distribution and telomere length (PMID:31664887, PMID:34301768). Beyond RNA metabolism, NOLC1 acts as a transcriptional co-activator, interacting with C/EBPbeta and TFIIB and mediating PKA signaling to the AGP gene, and engaging the TP53/MDM2 axis (PMID:8972203, PMID:12167624, PMID:19541936, PMID:40864495). NOLC1 protein and message are tuned by SPOP-mediated ubiquitination and FTO/m6A-dependent mRNA destabilization, with dysregulated levels driving nucleolar stress, p53 accumulation, and cellular senescence (PMID:40097806, PMID:41301545, PMID:41195691).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 1992 High

    Established Nopp140 as a nucleolar phosphoprotein that physically shuttles between nucleolus and cytoplasm, framing it as a candidate trafficking factor rather than a static structural component.

    Evidence Immunoelectron microscopy, subcellular fractionation, and pulse-chase shuttling in vertebrate cells

    PMID:1623516

    Open questions at the time
    • Cargo carried along the shuttling tracks not identified
    • Functional consequence of shuttling for ribosome biogenesis unresolved at this stage
  2. 1996 High

    Identified CK2 as the kinase responsible for Nopp140's extreme phosphorylation and showed conservation to the yeast homolog SRP40, establishing a conserved kinase-substrate relationship.

    Evidence In vitro kinase assays plus yeast overexpression/deletion growth assays

    PMID:8702624

    Open questions at the time
    • Functional purpose of hyperphosphorylation not yet defined
    • Specific serines mapped only later
  3. 1997 Medium

    Defined a direct, mapped physical interaction between Nopp140 and CK2, and independently revealed a transcriptional co-activator function via C/EBPbeta and TFIIB, broadening Nopp140 beyond a purely nucleolar role.

    Evidence GST pulldown, co-IP, overlay, deletion mapping (CK2beta); immunoaffinity, co-IP, reporter assays (C/EBPbeta, TFIIB)

    PMID:8972203 PMID:9013635

    Open questions at the time
    • Whether nucleolar and transcriptional co-activator pools are functionally distinct unresolved
    • Co-activator findings from single lab
  4. 1998 High

    Showed Nopp140 is the molecular link between nucleolus and Cajal bodies through its charged repeat domain and direct coilin interaction, explaining shared antigen distribution between the two compartments.

    Evidence Yeast two-hybrid, reciprocal co-IP, dominant-negative chase experiments

    PMID:9679133

    Open questions at the time
    • Mechanism of dual targeting by the same repeat domain not resolved
    • Stoichiometry of coilin-Nopp140 contacts unknown
  5. 1999 High

    Connected Nopp140 to RNA Pol I and rDNA transcription, establishing an essential role in pre-rRNA synthesis via interaction with the largest Pol I subunit.

    Evidence Co-IP interaction mapping (aa 204-382), run-on transcription, dominant-negative mislocalization of Pol I

    PMID:10567578

    Open questions at the time
    • Whether the effect is direct on Pol I or indirect via nucleolar integrity not separated
    • Dominant-negative may have pleiotropic effects
  6. 2000 High

    Demonstrated Nopp140 associates with both H/ACA and C/D snoRNPs and that its loss depletes snoRNPs from nucleoli and arrests Pol I transcription, positioning it as a snoRNP chaperone coupling modification machinery to transcription.

    Evidence Co-IP, dominant-negative transfection, yeast conditional depletion, northern blot

    PMID:10679015

    Open questions at the time
    • Whether snoRNP depletion causes or follows transcription arrest unresolved
    • Direct vs. scaffold-mediated snoRNP binding not distinguished
  7. 2002 High

    Distinguished Nopp140's chaperone role from catalysis by showing immunopurified H/ACA snoRNP cores pseudouridylate rRNA independently of Nopp140, and separately linked PKA phosphorylation to its transcriptional co-activation.

    Evidence In vitro reconstituted pseudouridylation assay; PKA-site mutagenesis and PKI reporter assays

    PMID:12167624 PMID:12446766

    Open questions at the time
    • The cellular advantage conferred by Nopp140 chaperoning of catalytically self-sufficient snoRNPs unresolved
    • PKA-dependence shown only for the AGP gene context
  8. 2008 High

    Quantified the Nopp140-CK2alpha interaction (Kd ~4 nM) and revealed Nopp140 as a CK2 inhibitor regulated by IP6, recasting the kinase-substrate pair as a mutually regulatory module.

    Evidence Surface plasmon resonance, yeast two-hybrid, CK2 activity assays, deletion mapping

    PMID:18790693

    Open questions at the time
    • In vivo significance of CK2 inhibition by Nopp140 not established
    • IP6 regulation tested biochemically, not in cells
  9. 2013 High

    Provided structural basis for Nopp140/IP6 competition at the CK2alpha substrate site and showed phospho-Ser574 enhances binding, mechanistically linking Nopp140's own phosphorylation to its CK2-regulatory activity.

    Evidence X-ray crystallography of CK2-IP6, competitive binding, CK2alpha mutagenesis, kinase assays

    PMID:24218616

    Open questions at the time
    • Co-structure of full Nopp140 with CK2 not determined
    • Cellular consequences of the lysine-cluster mutations untested
  10. 2009 Medium

    Linked Nopp140 CB localization to SMN and tied NOLC1 to the TP53-MDM2 transcriptional axis, expanding its connections to disease-relevant pathways.

    Evidence SMN knockdown/overexpression in SMA fibroblasts with immunofluorescence; ChIP, co-transfection, shRNA, NPC xenograft

    PMID:19129172 PMID:19541936

    Open questions at the time
    • Whether SMN directly recruits Nopp140 or acts via CB integrity unclear
    • MDM2 co-activation mechanism (direct DNA binding vs. p53 cofactor) not fully resolved
    • Both findings single-lab
  11. 2017 Medium

    Identified NOLC1 as a regulator of nucleolar TRF2 retention and showed its overexpression triggers a DNA damage response, linking NOLC1 to telomere protein compartmentalization and genome stability.

    Evidence Co-IP, siRNA, overexpression, immunofluorescence, TRF2 rescue of NOLC1-induced arrest

    PMID:28875039

    Open questions at the time
    • Cell-cycle dependence mechanism of TRF2 retention undefined
    • Single lab, two cell lines
  12. 2018 Medium

    Established Nopp140 as an intrinsically disordered protein whose CK2alpha-binding C-terminal segment undergoes disorder-to-rigidity transition upon binding, providing a physical basis for its scaffolding behavior.

    Evidence Single-molecule FRET, EPR with spin labeling, SPR

    PMID:29382046

    Open questions at the time
    • Conformational behavior of full-length protein not characterized
    • Link between disorder and condensate function not yet drawn here
  13. 2019 High

    Showed Nopp140 recruits and retains all scaRNPs in Cajal bodies and controls telomerase distribution and telomere length, defining it as the master organizer of CB RNP content.

    Evidence siRNA knockdown, CB granule EM, telomere length assays, immunofluorescence

    PMID:31664887

    Open questions at the time
    • How a single protein retains diverse scaRNPs mechanistically unresolved
    • Telomere effect mechanism via telomerase mislocalization not fully defined
  14. 2021 High

    Connected CK2 phosphorylation (~80 serines) to Nopp140's CB targeting and showed scaRNP retention is required for snRNA 2'-O-methylation and splicing fidelity, establishing CBs as the catalytic site for these modifications.

    Evidence Knockdown, snRNA 2'-O-methylation profiling, splicing analysis, phospho-site characterization

    PMID:34301768

    Open questions at the time
    • Which specific serines drive CB targeting not individually resolved
    • Magnitude of splicing defects across transcriptome not fully quantified
  15. 2022 High

    Defined the biophysical basis of CB assembly as multivalent coilin-NTD/Nopp140 condensation and embedded NOLC1 in additional nucleolar complexes (FGF12-NOLC1-TCOF1) and signaling axes (ACKR3/beta-arrestin-1 to fibrillarin), tying scaffolding to ribosome biogenesis regulation.

    Evidence Single-aa mutagenesis with live imaging and Nopp140 knockdown (coilin); co-IP and domain mapping (FGF12/TCOF1); co-IP, nuclear fractionation, transgenic mouse (ACKR3/beta-arr1)

    PMID:35365782 PMID:36224177 PMID:36411431

    Open questions at the time
    • Functional output of the FGF12-NOLC1-TCOF1 complex unresolved
    • ACKR3/beta-arr1 axis findings single-lab and Medium confidence
    • Relationship between coilin condensation and nucleolar phase separation unclear
  16. 2025 Medium

    Integrated NOLC1 into a phase-separation model of the dense fibrillar component and revealed layered control of its abundance (SPOP ubiquitination, FTO/m6A mRNA stability) with downstream consequences for transcription, glycosylation, p53-mediated ferroptosis, and senescence.

    Evidence Live imaging/phase separation and rRNA modification assays (preprint); ubiquitination and B4GALT1 reporter assays; m6A/RNA-stability and p53 assays; co-IP domain mapping and ferroptosis assays; R-ChIP and NPRA rescue senescence assays

    PMID:40097806 PMID:40864495 PMID:41195691 PMID:41301545

    Open questions at the time
    • DFC phase-separation model is a preprint and unreviewed
    • Whether NOLC1 acts as a sequence-specific transcription factor (B4GALT1, NPR1) or an adaptor cofactor is not resolved
    • p53/ferroptosis and senescence roles each from single labs in specific disease contexts

Open questions

Synthesis pass · forward-looking unresolved questions
  • How a single intrinsically disordered protein selectively partitions among its many functions — nucleolar DFC scaffolding, CB assembly, snoRNP/scaRNP chaperoning, Pol I support, and sequence-specific transcriptional regulation — and how phosphorylation state and abundance route it between these activities remains unresolved.
  • No structural model of full-length NOLC1 in any functional complex
  • No unified map linking specific phospho-states to specific localization/activity outcomes
  • Whether transcriptional 'co-activation' reflects direct DNA binding or scaffolding remains unclear

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140110 transcription regulator activity 5 GO:0003723 RNA binding 3 GO:0044183 protein folding chaperone 3 GO:0060090 molecular adaptor activity 3 GO:0098772 molecular function regulator activity 2
Localization
GO:0005730 nucleolus 3 GO:0005634 nucleus 2 GO:0005829 cytosol 1
Pathway
R-HSA-74160 Gene expression (Transcription) 4 R-HSA-8953854 Metabolism of RNA 4 R-HSA-1852241 Organelle biogenesis and maintenance 2 R-HSA-8953897 Cellular responses to stimuli 2
Partners
CEBPBCOILCSNK2A1CSNK2BFBLRPA194TFIIBTRF2
Complex memberships
Cajal bodyFGF12-NOLC1-TCOF1 complexbox C/D snoRNPbox H/ACA snoRNP

Evidence

Reading pass · 27 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1992 Nopp140 is a nucleolar phosphoprotein that shuttles between the nucleolus and cytoplasm on tracks revealed by immunoelectron microscopy, extending from the dense fibrillar component of the nucleolus across the nucleoplasm to nuclear pore complexes. It was identified as a nuclear localization signal (NLS)-binding protein whose NLS binding is dependent on phosphorylation. It is phosphorylated to an unusually high degree, with a 10-fold repeated motif containing casein kinase II (CK2) consensus sites. Immunoelectron microscopy, subcellular fractionation, biochemical characterization, pulse-chase shuttling assay Cell High 1623516
1996 Casein kinase II (CK2) phosphorylates Nopp140 to its unusually high degree in vertebrates; the yeast homolog SRP40 is also phosphorylated by CK2 but to a much lesser extent. SRP40 localizes to the yeast nucleolus and is required at a specific cellular concentration for optimal growth. In vitro kinase assay, immunological characterization, yeast growth assays (overexpression and deletion) The Journal of biological chemistry High 8702624
1997 Nopp140 interacts directly with the CK2 regulatory beta subunit; the NH2-terminal 20 amino acids of CK2beta mediate binding to Nopp140. Co-immunoprecipitation confirmed in vivo association of Nopp140 with CK2. GST pulldown with immobilized CK2 fusion proteins, co-immunoprecipitation, overlay technique with radiolabeled CK2, deletion mutant mapping The Journal of biological chemistry High 9013635
1997 Nopp140 functions as a transcriptional coactivator: it interacts with AGP/EBP (C/EBP beta) to synergistically activate the alpha-1 acid glycoprotein (AGP) gene, and independently interacts with TFIIB. Distinct regions of Nopp140 mediate interactions with AGP/EBP and TFIIB, and this physical interaction with TFIIB correlates with transcriptional activation ability. Immunoaffinity chromatography, co-immunoprecipitation, deletion mutant analysis, transcriptional reporter assays Molecular and cellular biology Medium 8972203
1998 Nopp140 functions as a molecular link between the nucleolus and coiled bodies (Cajal bodies): its alternating positively and negatively charged repeat domain is required for targeting to both organelles. Nopp140 directly interacts with the coiled body-specific protein p80 coilin, as identified by yeast two-hybrid screening and confirmed by co-immunoprecipitation. Dominant-negative Nopp140 constructs chase endogenous Nopp140 and shared antigens out of the nucleolus. Yeast two-hybrid screen, co-immunoprecipitation, transient transfection with dominant-negative constructs, mutational analysis The Journal of cell biology High 9679133
1999 Human Nopp140 (hNopp140) interacts with the largest subunit of RNA polymerase I (RPA194); this interaction is mediated through amino acids 204–382 of hNopp140. Expression of a dominant-negative hNopp140N382 (aa 1–382) mislocalizes endogenous RNA Pol I and shuts off rDNA transcription, establishing an essential role for Nopp140 in rDNA transcription. Co-immunoprecipitation, double immunofluorescence, in situ run-on transcription assay, dominant-negative transfection with deletion mapping Molecular and cellular biology High 10567578
2000 Nopp140 interacts with both box H/ACA snoRNPs (containing NAP57/dyskerin) and box C/D snoRNPs (containing NAP65/Nop5/58p) via co-immunoprecipitation. Dominant-negative Nopp140 depletes snoRNP proteins from nucleoli in vivo, and this depletion arrests RNA Pol I transcription. In yeast, depletion of the Nopp140 homolog Srp40p causes loss of box H/ACA snoRNAs. Co-immunoprecipitation, dominant-negative transfection, yeast conditional lethal depletion strain, northern blotting Molecular biology of the cell High 10679015
2001 Exogenous expression of the repeat domain of Nopp140 induces formation of intranuclear endoplasmic reticulum stacks (R-rings) derived from the inner nuclear membrane; Nopp140 localizes directly to the electron-dense matrix in which these membrane stacks are embedded, demonstrating a direct role for Nopp140 in generating this intranuclear membrane structure. Transmission electron microscopy, immunofluorescence, subcellular fractionation, exogenous expression of Nopp140 constructs Journal of cell science Medium 11739657
2002 Immunopurified box H/ACA snoRNP core particles (NAP57, GAR1, NHP2, NOP10) are sufficient for rRNA pseudouridylation in vitro. Although snoRNPs associate quantitatively and reversibly with Nopp140, pseudouridylation activity is independent of Nopp140 association, consistent with a chaperoning rather than catalytic role for Nopp140. In vitro pseudouridylation assay with immunopurified snoRNPs, thin-layer chromatography, 32P-labeled rRNA substrates Molecular and cellular biology High 12446766
2002 Nopp140 mediates protein kinase A (PKA) signaling to activate the AGP gene: PKA-dependent phosphorylation of Nopp140, together with C/EBPbeta, synergistically induces agp gene expression. Nopp140 mutants defective in PKA phosphorylation sites lose this transcriptional activation ability, and maximum activation also requires CREB and C/EBPbeta. Transcriptional reporter assays, PKA inhibitor (PKI) experiments, site-directed mutagenesis of PKA phosphorylation sites, co-transfection assays The Journal of biological chemistry Medium 12167624
2008 Nopp140 specifically binds to the catalytic subunit of CK2 (CK2alpha) with a dissociation constant of ~4 nM and inhibits CK2 catalytic activity. The C-terminal region of Nopp140 contains the CK2alpha-binding region. IP6 (inositol hexakisphosphate) specifically binds to CK2alpha and disrupts the Nopp140-CK2alpha interaction (IC50 ~25 µM), thereby relieving Nopp140-mediated inhibition of CK2. Surface plasmon resonance (quantitative binding assay), yeast two-hybrid, CK2 activity assays, deletion mutant mapping Biochemical and biophysical research communications High 18790693
2009 SMN (survival motor neuron protein) is required for accumulation of Nopp140 in Cajal bodies: SMN knockdown decreases Nopp140 in CBs, while SMN overexpression in SMA cells restores CB localization of Nopp140. SMA patient-derived SMN mutants fail to promote Nopp140 association with CBs. RNA interference knockdown of SMN, overexpression of wild-type and mutant SMN in SMA patient fibroblasts, immunofluorescence microscopy Human molecular genetics Medium 19129172
2009 NOLC1 is required for TP53-mediated activation of the MDM2 promoter: co-transfection and chromatin immunoprecipitation experiments showed that TP53-regulated expression of MDM2 requires co-activation by NOLC1. NOLC1 knockdown in NPC xenografts reduces tumor growth and induces apoptosis with downregulation of MDM2. Co-transfection reporter assays, chromatin immunoprecipitation (ChIP), shRNA knockdown, xenograft tumor model The American journal of pathology Medium 19541936
2013 Crystal structure of CK2 complexed with IP6 reveals that a lysine-rich cluster of CK2 is critical for IP6 binding. Biochemical experiments show that a Nopp140 fragment (residues 568–596) and IP6 competitively bind to CK2alpha at the substrate recognition site; phospho-Ser574 of Nopp140 significantly enhances its interaction with CK2alpha. Mutations K74E, K76E, K77E in CK2alpha reduce interactions with both IP6 and the Nopp140-derived peptide. X-ray crystallography, competitive binding assays, site-directed mutagenesis of CK2alpha, in vitro kinase activity assays, peptide-based interaction studies Proceedings of the National Academy of Sciences of the United States of America High 24218616
2014 Drosophila Nopp140 deletion causes redistribution of the C/D snoRNP methyltransferase fibrillarin to the nucleoplasm, reduced 2'-O-methylation of rRNA at select sites, loss of cytoplasmic ribosomes (replaced by abnormal electron-dense granules), loss of RpL34, and a significant drop in protein translation. Pre-rRNA cleavage pathways are generally unaffected. R2 retrotransposons within rDNA are selectively expressed upon Nopp140 loss. FLP-FRT gene deletion, immunofluorescence, RT-PCR, northern blot, metabolic labeling, immunoblot, ultrastructural analysis (TEM) Chromosoma High 25384888
2017 NOLC1 interacts with TRF2 and mediates nucleolar retention of TRF2 in a cell cycle-dependent manner. NOLC1 ablation increases nuclear TRF2 foci and decreases nucleolar TRF2 levels; conversely, NOLC1 overexpression promotes nucleolar accumulation of TRF2. NOLC1 overexpression also increases 53BP1 foci and induces DNA damage response; co-expression of TRF2 rescues NOLC1 overexpression-induced cell cycle arrest and apoptosis. Co-immunoprecipitation, siRNA knockdown, overexpression, immunofluorescence microscopy in 293T and HepG2 cells Cell death discovery Medium 28875039
2018 Nopp140 is an intrinsically disordered protein; its C-terminal region (residues 568–596, specifically residues 574–589) binds CK2alpha, and this interaction induces conformational rigidity in the otherwise disordered Nopp140 C-terminal region. Single-molecule FRET (smFRET), electron paramagnetic resonance (EPR) with site-specific spin labeling, surface plasmon resonance International journal of molecular sciences Medium 29382046
2019 Nopp140 is required to recruit and retain all scaRNPs (small Cajal body-specific RNPs) in Cajal bodies. Knockdown of Nopp140 releases all scaRNPs, causing an unprecedented reduction in size of CB granules. Mislocalization of telomerase by Nopp140 KD (as opposed to WDR79/TCAB1 mutation) leads to gradual extension of telomeres, identifying Nopp140 as a player in telomere length maintenance through dynamic distribution of telomerase between CBs and nucleoplasm. siRNA knockdown of Nopp140, electron microscopy (CB granule ultrastructure), telomere length assays, immunofluorescence Molecular biology of the cell High 31664887
2021 CB localization of Nopp140 is essential for scaRNP concentration in Cajal bodies, and phosphorylation by CK2 at ~80 serines targets Nopp140 to CBs. Nopp140 knockdown-mediated release of scaRNPs from CBs severely compromises 2'-O-methylation of spliceosomal snRNAs (U1, U2, U5, U12), identifying CBs as the site of scaRNP catalysis and establishing that these snRNA modifications safeguard splicing fidelity. Nopp140 knockdown, 2'-O-methylation profiling of snRNAs, alternative splicing analysis, CK2 phosphorylation site characterization Genes & development High 34301768
2022 Coilin's N-terminal domain (NTD) forms multivalent interactions with Nopp140 to achieve biomolecular condensation and CB assembly in the nucleus. Nopp140 has condensation capacity and is required for CB assembly; coilin NTD-NTD assemblies make multivalent contacts with Nopp140 to form nuclear puncta. Single amino acid mutations reveal distinct molecular interactions for fibril formation vs. Nopp140-dependent nuclear puncta formation. Single amino acid mutational analysis, live-cell imaging of coilin NTD behaviors (fibril vs. puncta formation), knockdown of Nopp140, in vivo condensation assays Nature communications High 36224177
2022 FGF12 is a nucleolar protein that interacts with both NOLC1 and TCOF1, and is required to bridge the NOLC1-TCOF1 interaction (NOLC1 and TCOF1 cannot interact with each other in the absence of FGF12). The FGF12-NOLC1-TCOF1 complex formation is phosphorylation-dependent and requires the C-terminal region of FGF12. Co-immunoprecipitation, nucleolar localization assays, deletion/domain analysis, phosphorylation-dependence experiments Cell communication and signaling : CCS Medium 36411431
2022 ACKR3 activation induces nuclear translocation of beta-arrestin-1 (beta-arr1), which interacts with NOLC1. Phosphorylated NOLC1 then interacts with fibrillarin (a nucleolar methyltransferase), increasing histone H2A methylation and promoting rRNA transcription in ribosome biogenesis. Co-immunoprecipitation, nuclear fractionation, CXCL12/AMD3100 pharmacological activation of ACKR3, transgenic mouse model, rRNA transcription assays Acta pharmacologica Sinica Medium 35365782
2025 SPOP (E3 ubiquitin ligase adaptor) mediates ubiquitination and proteasomal degradation of NOLC1 to maintain normal protein levels. ECa-associated SPOP mutants abrogate binding and ubiquitination of NOLC1, causing NOLC1 accumulation. NOLC1 acts as a transcriptional factor to activate transcription of B4GALT1, leading to abnormal glycosylation. Co-immunoprecipitation, ubiquitination assays, SPOP mutant expression, transcriptional reporter assays for B4GALT1, knockdown/overexpression experiments Oncogene Medium 40097806
2025 NOLC1 binds to the p53 DNA-binding domain (DBD), decreasing p53 nuclear accumulation stimulated by cisplatin and suppressing p53 transcriptional functions, thereby suppressing p53-mediated ferroptosis. Co-immunoprecipitation with domain mapping, NOLC1 knockdown, p53 nuclear accumulation assays, ferroptosis assays, p53 target gene expression analysis eLife Medium 40864495
2025 FTO (m6A eraser) destabilizes NOLC1 mRNA by removing m6A modifications; FTO knockdown increases m6A modifications on NOLC1 mRNA, increasing its stability and thus NOLC1 protein levels. Elevated NOLC1 inhibits pre-rRNA transcription, causing nucleolar stress and p53 accumulation, thereby promoting cellular senescence. m6A modification profiling, RNA stability assays, FTO knockdown/overexpression, NOLC1 knockdown rescue experiments, p53 accumulation assays, pre-rRNA transcription assays Biomolecules Medium 41301545
2025 Nopp140 concentrates intrinsically disordered, NLS-rich protein regions (IDRs) in the dense fibrillar component (DFC) of the nucleolus, including the CTD of RNA Pol I-associated factor PAF49. This network forms the DFC as a liquid-liquid phase separated condensate that fosters rRNA modification with near-100% efficiency. Live-cell imaging, phase separation assays, knockdown experiments, rRNA modification analysis bioRxivpreprint Medium
2025 NOLC1 functions as a key transcriptional regulator of NPR1 (encoding NPRA) in endothelial cells: reverse ChIP of the NPR1 promoter identified NOLC1 as a binding protein, and NOLC1 knockdown decreases both NPRA mRNA and protein expression. Loss of NOLC1 also triggers cellular senescence (elevated p53/p21, SA-β-gal, ROS, G0/G1 arrest), which is rescued by NPRA overexpression. Reverse chromatin immunoprecipitation (R-ChIP), siRNA knockdown, NPRA overexpression rescue experiments, senescence assays Genesis (New York, N.Y. : 2000) Medium 41195691

Source papers

Stage 0 corpus · 56 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1992 Nopp140 shuttles on tracks between nucleolus and cytoplasm. Cell 370 1623516
1998 Nopp140 functions as a molecular link between the nucleolus and the coiled bodies. The Journal of cell biology 143 9679133
2000 Conserved composition of mammalian box H/ACA and box C/D small nucleolar ribonucleoprotein particles and their interaction with the common factor Nopp140. Molecular biology of the cell 97 10679015
1997 Specific interaction between casein kinase 2 and the nucleolar protein Nopp140. The Journal of biological chemistry 92 9013635
1999 Human Nopp140, which interacts with RNA polymerase I: implications for rRNA gene transcription and nucleolar structural organization. Molecular and cellular biology 83 10567578
1996 Comparison of the rat nucleolar protein nopp140 with its yeast homolog SRP40. Differential phosphorylation in vertebrates and yeast. The Journal of biological chemistry 70 8702624
2002 Immunopurified small nucleolar ribonucleoprotein particles pseudouridylate rRNA independently of their association with phosphorylated Nopp140. Molecular and cellular biology 59 12446766
1997 Identification and characterization of a nucleolar phosphoprotein, Nopp140, as a transcription factor. Molecular and cellular biology 59 8972203
1996 Transcriptional induction of the alpha-1 acid glycoprotein (AGP) gene by synergistic interaction of two alternative activator forms of AGP/enhancer-binding protein (C/EBP beta) and NF-kappaB or Nopp140. Molecular and cellular biology 57 8754826
2001 Intranuclear endoplasmic reticulum induced by Nopp140 mimics the nucleolar channel system of human endometrium. Journal of cell science 48 11739657
2017 Enhanced NOLC1 promotes cell senescence and represses hepatocellular carcinoma cell proliferation by disturbing the organization of nucleolus. Aging cell 47 28493459
2021 Circ-NOLC1 promotes epithelial ovarian cancer tumorigenesis and progression by binding ESRP1 and modulating CDK1 and RhoA expression. Cell death discovery 43 33483472
2013 Structural and functional insights into the regulation mechanism of CK2 by IP6 and the intrinsically disordered protein Nopp140. Proceedings of the National Academy of Sciences of the United States of America 40 24218616
2009 NOLC1, an enhancer of nasopharyngeal carcinoma progression, is essential for TP53 to regulate MDM2 expression. The American journal of pathology 34 19541936
2017 Nucleolar and coiled-body phosphoprotein 1 (NOLC1) regulates the nucleolar retention of TRF2. Cell death discovery 32 28875039
1995 Identification and cDNA cloning of a Xenopus nucleolar phosphoprotein, xNopp180, that is the homolog of the rat nucleolar protein Nopp140. Journal of cell science 32 7593294
2021 A Zic2/Runx2/NOLC1 signaling axis mediates tumor growth and metastasis in clear cell renal cell carcinoma. Cell death & disease 30 33767130
2018 How Do We Study the Dynamic Structure of Unstructured Proteins: A Case Study on Nopp140 as an Example of a Large, Intrinsically Disordered Protein. International journal of molecular sciences 29 29382046
2022 The coilin N-terminus mediates multivalent interactions between coilin and Nopp140 to form and maintain Cajal bodies. Nature communications 27 36224177
2019 Nopp140-mediated concentration of telomerase in Cajal bodies regulates telomere length. Molecular biology of the cell 24 31664887
2014 Mutation of a Nopp140 gene dao-5 alters rDNA transcription and increases germ cell apoptosis in C. elegans. Cell death & disease 24 24722283
2009 The loss of the snoRNP chaperone Nopp140 from Cajal bodies of patient fibroblasts correlates with the severity of spinal muscular atrophy. Human molecular genetics 23 19129172
2022 FGF12 is a novel component of the nucleolar NOLC1/TCOF1 ribosome biogenesis complex. Cell communication and signaling : CCS 21 36411431
2014 Deletion of Drosophila Nopp140 induces subcellular ribosomopathies. Chromosoma 21 25384888
2011 Identification of nucleolar and coiled-body phosphoprotein 1 (NOLC1) minimal promoter regulated by NF-κB and CREB. BMB reports 21 21266110
2007 RNAi knockdown of Nopp140 induces Minute-like phenotypes in Drosophila. Molecular biology of the cell 21 17392509
2002 Two splice variants of Nopp140 in Drosophila melanogaster. Molecular biology of the cell 21 11809845
2018 Identification and validation of NOLC1 as a potential target for enhancing sensitivity in multidrug resistant non-small cell lung cancer cells. Cellular & molecular biology letters 20 30505321
2021 Nopp140-chaperoned 2'-O-methylation of small nuclear RNAs in Cajal bodies ensures splicing fidelity. Genes & development 18 34301768
2020 Pten-NOLC1 fusion promotes cancers involving MET and EGFR signalings. Oncogene 17 33323972
2013 Nucleolar stress in Drosophila melanogaster: RNAi-mediated depletion of Nopp140. Nucleus (Austin, Tex.) 17 23412656
2002 Nopp140 is a mediator of the protein kinase A signaling pathway that activates the acute phase response alpha1-acid glycoprotein gene. The Journal of biological chemistry 17 12167624
2009 Localization of Nopp140 within mammalian cells during interphase and mitosis. Histochemistry and cell biology 15 19381672
2005 Tracking nucleolar dynamics with GFP-Nopp140 during Drosophila oogenesis and embryogenesis. Cell and tissue research 13 16158326
2016 Three-Dimensional Distribution of UBF and Nopp140 in Relationship to Ribosomal DNA Transcription During Mouse Preimplantation Development. Biology of reproduction 12 26984997
2006 Characterization and differential nuclear localization of Nopp140 and a novel Nopp140-like protein in trypanosomes. Eukaryotic cell 12 16682465
2001 Ecto-protein kinase substrate p120 revealed as the cell-surface-expressed nucleolar phosphoprotein Nopp140: a candidate protein for extracellular Ca2+-sensing. The Biochemical journal 12 11736647
2023 Roles of NOLC1 in cancers and viral infection. Journal of cancer research and clinical oncology 11 37296317
2022 NOLC1 knockdown suppresses prostate cancer progressions by reducing AKT phosphorylation and β-catenin accumulation. Biochemical and biophysical research communications 10 36265288
2008 Characterization of the InsP6-dependent interaction between CK2 and Nopp140. Biochemical and biophysical research communications 9 18790693
2022 Atypical chemokine receptor 3 induces colorectal tumorigenesis in mice by promoting β-arrestin-NOLC1-fibrillarin-dependent rRNA biogenesis. Acta pharmacologica Sinica 8 35365782
2017 The interaction between NOLC1 and IAV NS1 protein promotes host cell apoptosis and reduces virus replication. Oncotarget 8 29212246
2015 Identification of NS1 domains of avian H5N1 influenza virus which influence the interaction with the NOLC1 protein. Virus genes 8 25645906
2019 The Nopp140 gene in Drosophila melanogaster displays length polymorphisms in its large repetitive second exon. Molecular genetics and genomics : MGG 5 31006039
2016 Biophysical characterization of the structural change of Nopp140, an intrinsically disordered protein, in the interaction with CK2α. Biochemical and biophysical research communications 5 27297113
2025 FOXA1 activates NOLC1 transcription through NOTCH pathway to promote cell stemness in lung adenocarcinoma. The Kaohsiung journal of medical sciences 4 39789998
2025 circ-NOLC1 inhibits the development of cervical cancer by regulating miR-330-5p-PALM signaling axis. Hereditas 3 40533863
2025 SPOP/NOLC1/B4GALT1 signaling axis enhances paclitaxel resistance in endometrial cancer by inducing O-dysglycosylation. Oncogene 2 40097806
2025 NOLC1 suppresses immunochemotherapy by inhibiting p53-mediated ferroptosis in gastric cancer. eLife 2 40864495
2024 Untangling Zebrafish Genetic Annotation: Addressing Complexities and Nomenclature Issues in Orthologous Evaluation of TCOF1 and NOLC1. Journal of molecular evolution 1 39269459
2021 Nopp140-chaperoned 2'-O-methylation of small nuclear RNAs in Cajal bodies ensures splicing fidelity. bioRxiv : the preprint server for biology 1 33948588
2025 CircRNA-NOLC1 mediates Insulin-like growth factor 1 receptor via performing as a ceRNA of miRNA-140-5p to facilitate testicular germ cell tumor advancement. Clinics (Sao Paulo, Brazil) 0 40367575
2025 NOLC1 as Key Regulator of NPR1 (Coding for NPRA) Transcription in Endothelial Senescence. Genesis (New York, N.Y. : 2000) 0 41195691
2025 FTO Suppresses Dental Pulp Stem Cell Senescence by Destabilizing NOLC1 mRNA. Biomolecules 0 41301545
2023 T7 phage display reveals NOLC1 as a GM3 binding partner in human breast cancer MCF-7 cells. Archives of biochemistry and biophysics 0 37939867
1999 Anisoosmotic regulation of the Nopp140 mRNA in H4IIE rat hepatoma cells and primary hepatocytes. FEBS letters 0 10386602

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