| 2005 |
PSPC1 (PSP1) forms a heterodimer with p54nrb (NONO) in vivo; the DBHS domain of PSPC1 mediates this interaction. This interaction is necessary but not sufficient for paraspeckle targeting, which also requires an RNA-binding-competent RRM domain. Paraspeckle formation itself is dependent on RNA Polymerase II transcription. |
Co-immunoprecipitation, domain-mapping experiments, DRB-mediated transcription inhibition assay, fluorescence microscopy |
Molecular biology of the cell |
High |
16148043
|
| 2006 |
PSPC1 interacts with androgen receptor (AR) and with NONO and SFPQ in Sertoli cells, forming complexes that coactivate AR-mediated transcription; PSPC1 is the most effective coactivator among the three DBHS proteins in this context. |
Co-immunoprecipitation, luciferase reporter assay with androgen-responsive elements, immunohistochemistry of mouse testis sections |
Biology of reproduction |
Medium |
16641145
|
| 2011 |
The PSPC1–NONO heterodimer was crystallized, confirming that the conserved DBHS domain (comprising two tandem RRMs, a NOPS domain, and part of a coiled-coil) provides the dimerization interface for these two paraspeckle proteins. |
Protein crystallography (crystal diffraction to 1.9 Å, space group C2) |
Acta crystallographica. Section F, Structural biology and crystallization communications |
Medium |
22102035
|
| 2013 |
PSPC1 is part of a transcriptional complex with LMX1B and PSF (SFPQ) in dopaminergic cells; PSPC1 was identified as a binding partner of LMX1B by affinity purification/mass spectrometry and confirmed by co-immunoprecipitation in vitro and in vivo. |
Affinity purification of LMX1B-HIS followed by mass spectrometry; co-immunoprecipitation in vitro and in vivo |
PloS one |
Medium |
23308148
|
| 2014 |
PSPC1 is required for the G1/S DNA damage checkpoint: knockdown of PSPC1 in HeLa cells caused cells to escape cisplatin-induced G1/S arrest and enter mitosis, leading to increased cell death. PSPC1 did not co-localize with γH2AX, 53BP1, or Rad51, indicating it does not directly participate in those DNA repair pathways. |
siRNA knockdown, cell cycle analysis by flow cytometry, γH2AX/53BP1/Rad51 co-localization by immunofluorescence, cisplatin treatment |
PloS one |
Medium |
24819514
|
| 2014 |
PSPC1 functionally compensates for NONO in DNA double-strand break (DSB) repair: in NONO-knockout MEFs, PSPC1 is upregulated and replaces NONO in a stable complex with SFPQ. Dual knockdown of NONO and PSPC1 causes severe radiosensitivity and delayed DSB repair focus resolution. Epistasis with DNA-PK inhibitor NU7741 places NONO/PSPC1 in the same DSB repair pathway as DNA-PK. |
Knockout mouse-derived MEFs, siRNA knockdown, clonogenic radiosensitivity assay, γH2AX foci resolution, DNA-PK inhibitor epistasis, co-immunoprecipitation |
Nucleic acids research |
High |
25100870
|
| 2017 |
PSPC1 binds intronic and 3'-UTR regions of adipocyte RNAs (including EBF1 mRNA) via CLIP-seq; it associates with the RNA export factor DDX3X in a differentiation-dependent manner. During adipogenesis, PSPC1 relocates from the nucleus to the cytoplasm, coinciding with enhanced nuclear export of adipogenic RNAs. PSPC1 knockout in fat reduces lipid storage and confers resistance to diet-induced obesity. |
CLIP-seq, paraspeckle complex purification from adipocytes, co-immunoprecipitation with DDX3X, subcellular fractionation/live imaging, adipose-specific knockout mouse |
The Journal of clinical investigation |
High |
28192372
|
| 2017 |
NONO and PSPC1 synergistically activate transcription of Aldh1a1 in Sertoli cells by binding to a specific CCGGAGTC sequence in the Aldh1a1 promoter, protecting cells against MEHP-induced oxidative stress. |
siRNA knockdown of NONO and PSPC1, promoter-binding assay, gene expression analysis, oxidative stress assay |
FEBS letters |
Medium |
28117896
|
| 2018 |
PSPC1 interacts with phosphorylated nuclear Smad2/3 to potentiate TGF-β1 autocrine signalling, increasing TGF-β1 secretion. PSPC1 acts as a contextual determinant of Smad2/3 binding preference, switching Smad2/3 from tumour-suppressor to pro-metastatic target genes, thereby driving EMT, stemness, and metastasis. |
Co-immunoprecipitation of PSPC1 with pSmad2/3, TGF-β1 ELISA, ChIP-seq for Smad2/3 binding, spontaneous mouse cancer models, multiple cancer cell lines |
Nature cell biology |
High |
29593326
|
| 2018 |
Crystal structure of the SFPQ/PSPC1 heterodimer resolved to 2.3 Å reveals that SFPQ-containing heterodimers dissociate at low micromolar concentrations and that SFPQ/PSPC1 heterodimer has >6-fold higher affinity than SFPQ/NONO heterodimer, providing a structural mechanism for preferential PSPC1–SFPQ heterodimerization over SFPQ homodimerization. |
X-ray crystallography (2.3 Å resolution), analytical ultracentrifugation |
The Journal of biological chemistry |
High |
29530979
|
| 2018 |
PSPC1 (PSP1/p54nrb) is required for HDV replication in HEK-293 cells; HDV replication induces delocalization of PSP1 from paraspeckles to cytoplasmic foci containing PABP and increases NEAT1 levels, causing paraspeckle enlargement. |
RNAi-mediated knockdown in HDV-replicating HEK-293 cells, immunofluorescence for PSP1 localization, NEAT1 level quantification |
Scientific reports |
Medium |
29662142
|
| 2019 |
PSPC1 is a nuclear substrate of PTK6; when PSPC1 sequesters PTK6 in the nucleus, PTK6 acts as a tumour suppressor. PSPC1 overexpression or Y523F mutation promotes cytoplasmic translocation of active PTK6 and nuclear translocation of β-catenin, which interacts with PSPC1 to augment Wnt3a autocrine signalling and drive EMT and metastasis. Expression of PSPC1-CT131 (C-terminal 131 aa) reverses these translocations and suppresses metastasis. |
Co-immunoprecipitation, subcellular fractionation, site-directed mutagenesis (Y523F), HCC orthotopic mouse model, PSPC1-CT131 peptide expression |
Nature communications |
High |
31844057
|
| 2020 |
PSPC1 overexpression induces focal adhesion formation and activates FAK/Src signalling to enhance cell adhesion and motility. PSPC1 transcriptionally upregulates IGF1R, which mediates focal adhesion pathway activation. Knockdown of paraspeckle components NONO, FUS, and NEAT1 lncRNA abolishes PSPC1-activated IGF1R expression. |
Phospho-kinase antibody array, RNA-seq transcriptome analysis, protein pulldown proteomics, IGF1R siRNA/inhibitor treatment, NONO/FUS/NEAT1 siRNA knockdown |
Cells |
Medium |
32570949
|
| 2021 |
PSPC1 interacts with phosphatase PPP5C (PP5), and through this interaction regulates CHK1 phosphorylation. PSPC1 undergoes liquid-liquid phase separation via its prion-like domain (PrLD); deletion of PrLD abolishes phase separation and abrogates PSPC1's ability to regulate CHK1 phosphorylation, impairing mouse oocyte maturation. |
Co-immunoprecipitation (PSPC1–PPP5C), Western blot for CHK1 phosphorylation, PrLD deletion mutant analysis, in vitro phase separation assay, mouse oocyte maturation assay with knockdown |
Acta biochimica et biophysica Sinica |
Medium |
34490876
|
| 2022 |
Crystal structures of the human NONO and PSPC1 homodimers were determined, revealing conserved contacts and structural plasticity at the dimerization interface that explain dimer selectivity among DBHS paralogs. Solution X-ray scattering showed that nucleic acid binding is reliant on RRM1 of NONO, and a newly identified 'β-clasp' structure influences RRM1 orientation for cooperative RNA recognition. |
X-ray crystallography (NONO and PSPC1 homodimers), small-angle X-ray scattering (SAXS), biochemical nucleic acid binding experiments |
Nucleic acids research |
High |
34904671
|
| 2022 |
PSPC1 interacts with TET1 in embryonic stem cells and functionally associates with Polycomb repressive complex-2 (PRC2) at bivalent gene promoters; PSPC1 and TET1 repress bivalent gene expression, and during ESC-to-EpiLC transition they maintain PRC2 chromatin occupancy at bivalent promoters. |
Proteomics-based TET1 interactome mapping, genome-wide ChIP-seq for PSPC1, TET1, and PRC2, loss-of-function experiments in ESCs |
Cell reports |
Medium |
35675764
|
| 2023 |
PSPC1 is a regulatory subunit of the m6A demethylase ALKBH5, preferentially interacting with K235-acetylated ALKBH5 (acetylated by KAT8, deacetylated by HDAC7) to recruit m6A-modified mRNA and facilitate m6A erasure, thereby promoting tumorigenesis. |
Co-immunoprecipitation of PSPC1 with acetylated ALKBH5, m6A demethylation activity assays, site-directed mutagenesis at K235, KAT8/HDAC7 writer/eraser identification |
Nature communications |
High |
37369679
|
| 2024 |
SKP2 stabilizes PSPC1 by preventing TRIM21-mediated polyubiquitination and proteasomal degradation of PSPC1; SKP2 depletion results in PSPC1 polyubiquitination and degradation, and the SKP2/PSPC1 axis promotes PDAC cell migration. |
Co-immunoprecipitation, ubiquitination assays, SKP2 depletion by siRNA, SMIP004 (SKP2 inhibitor) treatment, migration assays |
Cancer letters |
Medium |
38360141
|
| 2024 |
PSPC1 binds directly to the SLIV region of the HCV IRES upon HCV infection, competing with ribosomal protein RPS5 for IRES binding; PSPC1 binding prevents ribosomal loading and inhibits HCV RNA translation. Partial silencing of PSPC1 increases HCV RNA in polysomes and enhances viral replication. |
Competition UV-crosslinking experiments, PSPC1 partial silencing (siRNA), polysome profiling, immunoprecipitation assays |
Viruses |
Medium |
38793620
|
| 2025 |
PSPC1 co-occupies chromatin with the transcription factor PU.1 in AML cells, activating a unique leukemic transcription program including NDC1. PSPC1 loss induces myeloid differentiation and abolishes leukemogenesis; PSPC1 is not required for normal hematopoiesis. |
ChIP-seq for cooperative chromatin binding of PSPC1 and PU.1, PSPC1 knockout/knockdown in human AML cells and mouse models, differentiation and proliferation assays |
Cell stem cell |
High |
39954676
|
| 2025 |
PSPC1 interacts with SMAD3 and promotes its phosphorylation; iron-induced downregulation of PSPC1 alleviates SMAD3-mediated repression of thermogenic genes, thereby inducing beiging of white adipocytes. Overexpression of PSPC1 in subcutaneous adipose tissue reverses iron-induced beiging. |
Co-immunoprecipitation of PSPC1 with SMAD3, RNA-seq and ATAC-seq in adipocytes, PSPC1 overexpression in vivo (subcutaneous adipose tissue), Western blot for SMAD3 phosphorylation |
Cell communication and signaling : CCS |
Medium |
41345872
|
| 2025 |
NONO, SFPQ, and PSPC1 associate with catalytically active telomerase through the hTR RNA component. Depletion of PSPC1 (and NONO) causes telomerase retention in Cajal bodies, impairs telomerase recruitment to telomeres, and leads to progressive telomere shortening. |
Co-immunoprecipitation of DBHS proteins with telomerase/hTR, immunofluorescence for Cajal body retention, telomere length measurement upon PSPC1/NONO depletion in multiple cell lines |
Nature communications |
High |
40593584
|
| 2025 |
PSPC1 interacts with PARP1, competitively inhibiting PARP1-mediated PARylation and dephosphorylation of STAT3, thereby sustaining STAT3 activation and promoting CCL2 transcription and M2 macrophage polarization. |
Co-immunoprecipitation of PSPC1 with PARP1, STAT3 phosphorylation assays, CCL2 secretion measurement, macrophage polarization co-culture assay |
Oncogene |
Medium |
41986651
|
| 2025 |
Etoposide-induced DNA double-strand breaks do not substantially alter the NONO–SFPQ or NONO–PSPC1 protein-protein interactions, indicating that DBHS family members promote genome stability as constitutively stable dimers rather than dynamically assembling upon DNA damage. |
Label-free mass spectrometry interactome profiling of NONO in U2OS cells ± etoposide, orthogonal co-immunoprecipitation, co-localization assays |
bioRxivpreprint |
Medium |
|