Affinage

PSPC1

Paraspeckle component 1 · UniProt Q8WXF1

Length
523 aa
Mass
58.7 kDa
Annotated
2026-04-28
46 papers in source corpus 26 papers cited in narrative 27 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PSPC1 is a DBHS-family nuclear scaffold protein that dimerizes through its conserved DBHS domain—preferentially forming heterodimers with SFPQ (Kd ~6-fold lower than SFPQ–NONO) and also with NONO—and binds RNA and DNA via tandem RRMs, functioning as a context-dependent transcriptional and post-transcriptional regulator across diverse cellular processes (PMID:16148043, PMID:29530979, PMID:27084935). PSPC1 acts as a contextual determinant of TGF-β1 signaling by interacting with phospho-Smad2/3 to redirect their binding from tumor-suppressive to pro-metastatic gene targets, controls Wnt signaling by sequestering PTK6 in the nucleus and regulating β-catenin nuclear translocation, cooperates with PU.1 at chromatin to sustain a leukemic transcription program essential for AML, and serves as a regulatory subunit of the ALKBH5 m6A demethylase by recruiting it to m6A-modified mRNAs (PMID:29593326, PMID:31844057, PMID:39954676, PMID:37369679). Beyond transcription, PSPC1 participates in DNA double-strand break repair in the DNA-PK epistasis pathway, facilitates telomerase trafficking from Cajal bodies to telomeres, and relocalizes to the cytoplasm during adipogenesis to promote DDX3X-dependent export of adipogenic RNAs, with fat-specific knockout mice showing reduced adiposity (PMID:25100870, PMID:40593584, PMID:28192372). PSPC1 protein stability is regulated by SKP2-mediated protection from TRIM21 polyubiquitination and proteasomal degradation, and its expression is transcriptionally controlled by NR4A1 (PMID:38360141, PMID:34699643).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2005 High

    Establishing that PSPC1 functions as a DBHS heterodimer: the DBHS domain mediates interaction with NONO, and both dimerization and RRM-dependent RNA binding are required for paraspeckle localization, linking PSPC1 to nuclear body organization.

    Evidence Co-immunoprecipitation with domain-mapping constructs, DRB transcription inhibition, and live-cell imaging in mammalian cells

    PMID:16148043

    Open questions at the time
    • Preference among possible DBHS dimer combinations not yet quantified
    • RNA targets mediating paraspeckle targeting not identified
    • Whether PSPC1 has functions independent of paraspeckles unknown
  2. 2006 Medium

    Revealing PSPC1 as a transcriptional coactivator: PSPC1 was the most potent DBHS-family coactivator of androgen receptor-mediated transcription in Sertoli cells, demonstrating a role beyond structural scaffolding.

    Evidence Co-immunoprecipitation and luciferase reporter assays with androgen-responsive elements in Sertoli cells

    PMID:16641145

    Open questions at the time
    • Direct DNA-binding versus indirect recruitment to AR target genes not resolved
    • Mechanism of coactivation (chromatin remodeling, Mediator recruitment) unknown
    • Not independently replicated in a second system
  3. 2011 High

    Defining the atomic architecture of the PSPC1–NONO dimer: crystallography revealed that the conserved DBHS core (tandem RRMs, NOPS, coiled-coil) forms the dimerization interface, providing a structural framework for understanding all DBHS interactions.

    Evidence X-ray crystallography at 1.9 Å resolution

    PMID:22102035

    Open questions at the time
    • Structure of RNA- or DNA-bound complexes not determined
    • How dimer selectivity arises from conserved interfaces not explained
  4. 2014 High

    Establishing PSPC1 as a DNA damage response effector: PSPC1 compensates for NONO loss by forming an alternative SFPQ complex, and combined NONO/PSPC1 depletion causes severe DSB repair deficiency epistatic with DNA-PK, placing PSPC1 in non-homologous end-joining.

    Evidence MEF knockout/knockdown, clonogenic survival, γH2AX foci, DNA-PK inhibitor epistasis

    PMID:24819514 PMID:25100870

    Open questions at the time
    • Direct biochemical role at DSBs (bridging, end-processing, recruitment) not defined
    • Whether PSPC1 acts through RNA binding or protein scaffolding at break sites unclear
  5. 2017 High

    Uncovering a cytoplasmic RNA-export function: PSPC1 binds intronic/3ʹ-UTR regions of adipogenic mRNAs, associates with DDX3X, and relocalizes to the cytoplasm during adipogenesis to promote RNA export; fat-specific PSPC1 knockout mice are lean and obesity-resistant.

    Evidence CLIP-seq, complex purification/MS, subcellular fractionation, adipose-specific knockout mouse

    PMID:28192372

    Open questions at the time
    • Mechanism by which PSPC1 releases from paraspeckles during differentiation not identified
    • Whether DDX3X is the sole export partner or one of several not resolved
  6. 2018 High

    Identifying PSPC1 as a master contextual switch of TGF-β signaling: PSPC1 interacts with phospho-Smad2/3 to redirect their binding from tumor-suppressor to pro-metastatic target genes, driving EMT and stemness across multiple cancer types.

    Evidence ChIP-seq, co-immunoprecipitation, luciferase reporters, CRISPR/siRNA, spontaneous mouse cancer models

    PMID:29593326

    Open questions at the time
    • Structural basis of PSPC1–Smad2/3 interaction not determined
    • Mechanism by which PSPC1 alters Smad2/3 genomic targeting not defined at chromatin level
  7. 2018 High

    Quantifying DBHS dimer selectivity: the SFPQ–PSPC1 heterodimer has >6-fold higher affinity than SFPQ–NONO, explaining how low-abundance PSPC1 can compete for SFPQ and form functionally distinct complexes.

    Evidence X-ray crystallography at 2.3 Å combined with analytical ultracentrifugation

    PMID:29530979

    Open questions at the time
    • Whether cellular concentrations permit complete SFPQ capture by PSPC1 in specific cell types not measured
    • Functional consequences of dimer preference on specific RNA/DNA targets not mapped
  8. 2019 High

    Linking PSPC1 to Wnt/β-catenin signaling via PTK6: unphosphorylated PSPC1 sequesters PTK6 in the nucleus; PSPC1 upregulation or Y523F mutation releases active PTK6 to the cytoplasm and promotes nuclear β-catenin accumulation, activating Wnt3a autocrine signaling and metastasis.

    Evidence Co-immunoprecipitation, Y523F mutagenesis, subcellular fractionation, Wnt luciferase reporter, orthotopic HCC mouse model

    PMID:31844057

    Open questions at the time
    • Whether PTK6-mediated phosphorylation of PSPC1 at Y523 occurs in all cancer types not tested
    • Stoichiometry of PSPC1–PTK6 versus PSPC1–β-catenin complexes unclear
  9. 2022 High

    Revealing PSPC1 as a chromatin co-regulator at bivalent promoters: PSPC1 co-localizes genome-wide with TET1 and PRC2 at bivalent gene promoters in ESCs, where it represses bivalent gene expression and maintains PRC2 occupancy during the ESC-to-EpiLC transition.

    Evidence TET1 interactome proteomics, ChIP-seq for PSPC1/TET1/PRC2, RNA-seq, siRNA/shRNA in ESCs

    PMID:35675764

    Open questions at the time
    • Whether PSPC1 directly contacts PRC2 or acts through TET1 not resolved
    • Mechanism by which PSPC1 opposes Neat1-mediated activation of bivalent genes not defined
  10. 2023 High

    Establishing PSPC1 as a regulatory subunit of the m6A demethylase ALKBH5: PSPC1 preferentially binds K235-acetylated ALKBH5 and recruits it to m6A-modified mRNAs, thereby promoting m6A erasure and linking PSPC1 to epitranscriptomic regulation.

    Evidence Co-immunoprecipitation, K235 acetylation mutagenesis, m6A quantification, RNA pull-down

    PMID:37369679

    Open questions at the time
    • Specific mRNA targets whose m6A status and fate are controlled by PSPC1–ALKBH5 not comprehensively mapped
    • Whether PSPC1 RNA-binding directs ALKBH5 to specific transcripts or acts more generally unknown
  11. 2024 Medium

    Defining PSPC1 protein turnover: SKP2 protects PSPC1 from TRIM21-mediated K48-polyubiquitination and proteasomal degradation, providing a mechanism for PSPC1 stabilization in metastatic cancers; separately, NR4A1 transcriptionally activates PSPC1 expression.

    Evidence Co-immunoprecipitation, ubiquitination assays, siRNA knockdown, ChIP at PSPC1 promoter, NR4A1 antagonist treatment

    PMID:34699643 PMID:38360141

    Open questions at the time
    • Whether SKP2 acts as a non-canonical E3 ligase or simply blocks TRIM21 access not mechanistically distinguished
    • Upstream signals regulating NR4A1-PSPC1 axis in specific cancer contexts not delineated
    • Both findings from single laboratories
  12. 2025 High

    Establishing PSPC1 as essential for AML but dispensable for normal hematopoiesis: PSPC1 cooperates with PU.1 at chromatin to activate a leukemogenic transcription program including NDC1; loss of PSPC1 induces differentiation and abolishes leukemogenesis.

    Evidence CRISPR KO, ChIP-seq for PSPC1/PU.1 co-binding, RNA-seq, mouse AML models, human AML xenografts

    PMID:39954676

    Open questions at the time
    • Whether PSPC1 directly contacts PU.1 or is recruited through shared chromatin features not resolved
    • Which PSPC1 domain is required for leukemogenic function not mapped
  13. 2025 High

    Connecting PSPC1 to telomere maintenance: DBHS proteins associate with catalytically active telomerase through hTR, and PSPC1/NONO depletion causes telomerase retention in Cajal bodies and progressive telomere shortening.

    Evidence Telomerase co-immunoprecipitation, Cajal body colocalization immunofluorescence, TRF Southern blot across multiple cell lines

    PMID:40593584

    Open questions at the time
    • Whether PSPC1 directly binds hTR or acts through NONO/SFPQ bridge not determined
    • Structural basis of DBHS–telomerase interaction unknown
    • Whether telomere shortening contributes to PSPC1 loss phenotypes in cancer models not tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • Open question: how PSPC1 is dynamically allocated among its many distinct complexes (Smad2/3, ALKBH5, PU.1, telomerase, β-catenin, TET1) in a cell-type and signal-dependent manner, and whether these represent mutually exclusive or co-existing interaction states.
  • No single-molecule or stoichiometric analysis of competing PSPC1 complexes performed
  • Post-translational modification code governing complex selection not systematically characterized
  • Separation-of-function mutations distinguishing individual PSPC1 roles not available

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 4 GO:0140110 transcription regulator activity 4 GO:0003677 DNA binding 3 GO:0060090 molecular adaptor activity 2 GO:0098772 molecular function regulator activity 2
Localization
GO:0005634 nucleus 5 GO:0005829 cytosol 3
Pathway
R-HSA-162582 Signal Transduction 4 R-HSA-1643685 Disease 3 R-HSA-74160 Gene expression (Transcription) 3 R-HSA-8953854 Metabolism of RNA 2
Partners
ALKBH5DDX3XNONOPTK6SFPQSMAD2SMAD3TET1
Complex memberships
DBHS heterodimer (PSPC1–NONO)DBHS heterodimer (PSPC1–SFPQ)PSPC1–ALKBH5 m6A eraser complex

Evidence

Reading pass · 27 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2005 PSPC1 (PSP1) forms a heterodimer with p54nrb (NONO) in vivo; the DBHS domain of PSPC1 mediates this interaction and is required for correct localization of PSPC1 to paraspeckles; both the heterodimer interaction and RNA-binding capability of RRM are necessary but individually insufficient for paraspeckle targeting; paraspeckle formation requires RNA Polymerase II transcription. Co-immunoprecipitation, domain-mapping constructs, DRB transcription inhibition, live-cell imaging/immunofluorescence Molecular biology of the cell High 16148043
2006 PSPC1, NONO, and SFPQ interact reciprocally and form complexes in Sertoli cells; all three proteins coactivate androgen receptor-mediated transcription, with PSPC1 being the most potent coactivator among them. Co-immunoprecipitation, luciferase reporter assay with androgen-responsive elements, immunofluorescence in mouse testis sections Biology of reproduction Medium 16641145
2011 The PSPC1-NONO heterodimer was crystallized and diffracted to 1.9 Å resolution, establishing that the core DBHS conserved region (two RRMs, NOPS domain, and coiled-coil segment) forms the structural basis of the heterodimer. Protein crystallography (X-ray diffraction, 1.9 Å resolution) Acta crystallographica. Section F High 22102035
2014 NONO deficiency causes upregulation of PSPC1, which replaces NONO in a stable complex with SFPQ; double knockdown of both NONO and PSPC1 causes severe radiosensitivity and impaired resolution of DNA double-strand break (DSB) repair foci; NONO/PSPC1 and DNA-PK function in the same DSB repair pathway (epistasis with DNA-PK inhibitor NU7741). MEF knockout/knockdown, clonogenic survival, γH2AX foci assay, DNA-PK inhibitor epistasis, co-immunoprecipitation Nucleic acids research High 25100870
2014 PSPC1 is required for the G1/S checkpoint response to cisplatin-induced DNA damage; knockdown of PSPC1 causes cells to bypass the G1/S checkpoint and enter mitosis, resulting in increased cell death, without direct co-localization with γH2AX, 53BP1, or Rad51 repair foci. siRNA knockdown, cell cycle analysis (flow cytometry), γH2AX/53BP1/Rad51 co-localization immunofluorescence PloS one Medium 24819514
2016 PSPC1, NONO, and SFPQ are described structurally and functionally as a DBHS family acting as multipurpose molecular scaffolds mediating protein-protein and protein-nucleic acid interactions; the DBHS domain provides a dimerization platform critical for structural integrity and function. Structural review integrating crystallographic data, nucleic acid binding assays, and functional studies Nucleic acids research High 27084935
2017 PSPC1 binds to intronic and 3'-UTR regions of adipocyte RNAs (including EBF1 mRNA) via CLIP-seq; associates with RNA export factor DDX3X in a differentiation-dependent manner; relocates from nucleus to cytoplasm during adipogenesis to promote export of adipogenic RNAs; mice lacking fat-specific PSPC1 show reduced adipose mass and resistance to diet-induced obesity. CLIP-seq, paraspeckle complex purification + MS, subcellular fractionation, nuclear/cytoplasmic co-immunoprecipitation, adipose-specific knockout mouse The Journal of clinical investigation High 28192372
2017 NONO and PSPC1 synergistically bind to the CCGGAGTC sequence in the Aldh1a1 promoter to transcriptionally activate ALDH1A1 in Sertoli cells, providing a defense mechanism against MEHP-induced oxidative stress. siRNA knockdown, luciferase reporter assay, chromatin immunoprecipitation (ChIP) FEBS letters Medium 28117896
2018 PSPC1 promotes TGF-β1 autocrine signaling by interacting with phosphorylated nuclear Smad2/3 to increase TGF-β1 secretion; PSPC1 acts as a contextual determinant of the TGF-β1 pro-metastatic switch by altering Smad2/3 binding preference from tumor-suppressor to pro-metastatic genes; PSPC1 also activates EMT/stemness transcription factors and accompanies c-Myc activation. Co-immunoprecipitation, ChIP-seq, luciferase reporters, CRISPR/siRNA knockdown, spontaneous mouse cancer models, TGF-β1 ELISA Nature cell biology High 29593326
2018 Crystal structure of the SFPQ/PSPC1 heterodimer resolved to 2.3 Å; analytical ultracentrifugation shows SFPQ/PSPC1 heterodimer has over 6-fold lower apparent dissociation constant than SFPQ/NONO heterodimer, providing a mechanism by which lower-abundance PSPC1 outcompetes NONO for SFPQ binding. X-ray crystallography (2.3 Å), analytical ultracentrifugation The Journal of biological chemistry High 29530979
2018 PSPC1 (PSP1) is required for Hepatitis Delta Virus (HDV) replication; HDV replication induces delocalization of PSP1 from paraspeckles to cytoplasmic foci (containing PABP) and increases NEAT1 levels causing paraspeckle enlargement. RNAi knockdown in HDV-replicating HEK-293 cells, immunofluorescence, NEAT1 quantification Scientific reports Medium 29662142
2019 PSPC1 is a nuclear substrate of PTK6; unphosphorylated PSPC1 sequesters PTK6 in the nucleus as a tumor suppressor. PSPC1 upregulation or PSPC1-Y523F mutation promotes cytoplasmic translocation of active PTK6 and nuclear translocation of β-catenin; nuclear β-catenin interacts with PSPC1 to augment Wnt3a autocrine signaling. The PSPC1 C-terminal domain (PSPC1-CT131) reverses PTK6/β-catenin shuttling and suppresses metastasis in HCC orthotopic mice. Co-immunoprecipitation, site-directed mutagenesis (Y523F), subcellular fractionation, luciferase Wnt reporter, orthotopic mouse model, immunofluorescence Nature communications High 31844057
2020 PSPC1 overexpression activates FAK/Src signaling and upregulates IGF1R expression to enhance focal adhesion formation, stress fiber assembly, and cell motility; knockdown of PSPC1-interacting paraspeckle components NONO, FUS, and lncRNA Neat1 abolishes PSPC1-activated IGF1R expression. Phospho-kinase antibody array, RNA-seq/transcriptome analysis, protein pulldown, IGF1R inhibitor treatment, siRNA knockdown Cells Medium 32570949
2021 PSPC1 undergoes liquid-liquid phase separation (LLPS) via its prion-like domain (PrLD); PSPC1 interacts with PPP5C (protein phosphatase 5) via co-IP; PSPC1 regulates CHK1 phosphorylation through PPP5C in a phase separation-dependent manner; knockdown of PSPC1 impedes mouse oocyte maturation in vitro. Phase separation assay (in vitro droplet formation), co-immunoprecipitation, Western blot (CHK1 phosphorylation), siRNA knockdown in mouse oocytes, immunofluorescence Acta biochimica et biophysica Sinica Medium 34490876
2022 Crystal structures of NONO and PSPC1 homodimers reveal conserved contacts and structural plasticity in the dimerization interface providing a rationale for dimer selectivity; solution X-ray scattering and biochemical experiments show cooperative RNA recognition by NONO homodimer dependent on RRM1 orientation, influenced by a newly identified 'β-clasp' structure. X-ray crystallography, solution small-angle X-ray scattering (SAXS), biochemical RNA-binding assays Nucleic acids research High 34904671
2022 PSPC1 interacts with TET1 in embryonic stem cells (ESCs); PSPC1 co-localizes genome-wide with TET1 and PRC2 at bivalent promoters; PSPC1 and TET1 repress bivalent gene expression while lncRNA Neat1 activates it; PSPC1 and TET1 maintain PRC2 chromatin occupancy at bivalent gene promoters during ESC-to-EpiLC transition. Co-immunoprecipitation/proteomics (TET1 interactome), ChIP-seq (PSPC1, TET1, PRC2), RNA-seq, siRNA/shRNA knockdown Cell reports High 35675764
2023 PSPC1 is a regulatory subunit of the m6A demethylase ALKBH5; PSPC1 preferentially interacts with K235-acetylated ALKBH5 (acetylated by KAT8, deacetylated by HDAC7); PSPC1 recruits and facilitates recognition of m6A mRNA by ALKBH5, thereby promoting m6A erasure. Co-immunoprecipitation, m6A quantification assay, mutagenesis (K235 acetylation site), RNA pull-down Nature communications High 37369679
2013 LMX1B forms a transcriptional complex with PSPC1 and PSF (SFPQ); this complex was identified by affinity-purification/MS and confirmed by co-immunoprecipitation in vitro and in vivo in dopaminergic cells. Affinity-purification mass spectrometry, co-immunoprecipitation (in vitro and in vivo) PloS one Medium 23308148
2024 SKP2 interacts with PSPC1 and protects it from TRIM21-mediated polyubiquitination and proteasomal degradation; SKP2 depletion results in TRIM21-dependent PSPC1 polyubiquitination and degradation, reducing metastasis of pancreatic ductal adenocarcinoma cells. Co-immunoprecipitation, ubiquitination assay, siRNA knockdown, migration assay Cancer letters Medium 38360141
2024 PSPC1 binds to the SLIV region of the HCV IRES via its RNA-binding domain (demonstrated by UV-crosslinking); this interaction prevents ribosomal protein S5 (RPS5) binding to SLIV, thereby inhibiting viral RNA translation and HCV replication; PSPC1 relocalizes from nucleus to cytoplasm upon HCV infection. UV-crosslinking competition assay, siRNA knockdown, polysome profiling, immunofluorescence (relocalization) Viruses Medium 38793620
2025 PSPC1 is critical for AML leukemogenesis but not normal hematopoiesis; PSPC1 cooperatively binds chromatin with PU.1 to regulate a leukemic transcription program, activating tumor-promoting genes including NDC1; PSPC1 loss induces differentiation and abolishes leukemogenesis in diverse AML cells and mouse models. CRISPR knockout, ChIP-seq (PSPC1 and PU.1 co-binding), RNA-seq, mouse AML models, human AML xenografts Cell stem cell High 39954676
2025 NONO, SFPQ, and PSPC1 (DBHS proteins) associate with catalytically active telomerase through the hTR RNA template component; depletion of NONO and PSPC1 causes telomerase retention in nuclear Cajal bodies, impairs telomerase recruitment to the telomere, and leads to progressive telomere shortening. Co-immunoprecipitation (telomerase pull-down), immunofluorescence (Cajal body colocalization), telomere length assays (Southern blot/TRF), siRNA/shRNA knockdown Nature communications High 40593584
2025 PSPC1 interacts with SMAD3 and promotes its phosphorylation; iron-induced downregulation of PSPC1 reduces SMAD3 phosphorylation, relieving its repression of thermogenic genes and inducing beiging of white adipocytes; overexpression of PSPC1 in subcutaneous adipose tissue reverses iron-induced SMAD3 dephosphorylation and beiging. RNA-seq, ATAC-seq, co-immunoprecipitation, Western blot (phospho-SMAD3), adeno-associated virus (AAV) overexpression in mice Cell communication and signaling Medium 41345872
2025 PSPC1 interacts with PARP1 in gastric cancer cells, competitively inhibiting PARP1-mediated PARylation and dephosphorylation of STAT3, thereby sustaining STAT3 phosphorylation and promoting CCL2 transcription to drive M2 macrophage polarization. Co-immunoprecipitation, PARylation assay, STAT3 phosphorylation Western blot, ChIP, cytokine ELISA Oncogene Medium 41986651
2021 NR4A1 transcriptionally regulates PSPC1 expression through binding to an NBRE sequence in the PSPC1 gene promoter, as shown by ChIP assay; NR4A1 antagonists downregulate PSPC1 and its downstream targets (TGFβ, EMT genes, cancer stem cell genes) in breast, lung, and liver cancer cells. Chromatin immunoprecipitation (ChIP), siRNA knockdown, NR4A1 antagonist treatment Molecular carcinogenesis Medium 34699643
2025 PSPC1 regulates matrix stiffness-dependent TGF-β1 signaling in kidney progenitor cells; on stiff matrices, TGF-β1 reduces Neat1 levels, releasing PSPC1 to interact with pSmad2/3 and activate EMT-related gene expression promoting myofibroblast activation; PSPC1 and Neat1 respond to mechanical signals via β1-integrin-YAP and Piezo1 pathways. siRNA/shRNA knockdown, overexpression, immunofluorescence, RNA-FISH, Western blot (pSmad2/3), RNA-seq Journal of biomedical science Medium 41243096
2025 DBHS protein interactions (NONO with SFPQ or PSPC1) are stable and do not change substantially upon etoposide-induced DNA double-strand breaks, suggesting DBHS family members promote genome stability as constitutive stable dimers. Label-free mass spectrometry (interactome), co-immunoprecipitation, co-localization assays bioRxivpreprint Medium

Source papers

Stage 0 corpus · 46 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2016 The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold. Nucleic acids research 268 27084935
2005 P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RNA-dependent manner. Molecular biology of the cell 196 16148043
2018 PSPC1 mediates TGF-β1 autocrine signalling and Smad2/3 target switching to promote EMT, stemness and metastasis. Nature cell biology 163 29593326
2006 PSPC1, NONO, and SFPQ are expressed in mouse Sertoli cells and may function as coregulators of androgen receptor-mediated transcription. Biology of reproduction 78 16641145
2014 Double-strand break repair deficiency in NONO knockout murine embryonic fibroblasts and compensation by spontaneous upregulation of the PSPC1 paralog. Nucleic acids research 59 25100870
2017 RNA-binding protein PSPC1 promotes the differentiation-dependent nuclear export of adipocyte RNAs. The Journal of clinical investigation 41 28192372
2023 K235 acetylation couples with PSPC1 to regulate the m6A demethylation activity of ALKBH5 and tumorigenesis. Nature communications 39 37369679
2019 PSPC1-interchanged interactions with PTK6 and β-catenin synergize oncogenic subcellular translocations and tumor progression. Nature communications 37 31844057
2018 Crystal structure of a SFPQ/PSPC1 heterodimer provides insights into preferential heterodimerization of human DBHS family proteins. The Journal of biological chemistry 37 29530979
2022 Structural basis of dimerization and nucleic acid binding of human DBHS proteins NONO and PSPC1. Nucleic acids research 29 34904671
2018 The Hepatitis Delta Virus accumulation requires paraspeckle components and affects NEAT1 level and PSP1 localization. Scientific reports 28 29662142
2016 FTIR imaging of the molecular burden around Aβ deposits in an early-stage 3-Tg-APP-PSP1-TAU mouse model of Alzheimer's disease. The Analyst 22 27917428
1997 A novel protein, Psp1, essential for cell cycle progression of Schizosaccharomyces pombe is phosphorylated by Cdc2-Cdc13 upon entry into G0-like stationary phase of cell growth. The Journal of biological chemistry 21 9242669
2024 SKP2 promotes the metastasis of pancreatic ductal adenocarcinoma by suppressing TRIM21-mediated PSPC1 degradation. Cancer letters 20 38360141
2022 A TET1-PSPC1-Neat1 molecular axis modulates PRC2 functions in controlling stem cell bivalency. Cell reports 20 35675764
2013 LMX1B is part of a transcriptional complex with PSPC1 and PSF. PloS one 18 23308148
2011 Construct optimization for studying protein complexes: obtaining diffraction-quality crystals of the pseudosymmetric PSPC1-NONO heterodimer. Acta crystallographica. Section D, Biological crystallography 18 22101825
2014 Paraspeckle protein 1 (PSPC1) is involved in the cisplatin induced DNA damage response--role in G1/S checkpoint. PloS one 17 24819514
2015 Advantages of the phosphatidylserine-recognizing peptide PSP1 for molecular imaging of tumor apoptosis compared with annexin V. PloS one 15 25803297
2020 PSPC1 Potentiates IGF1R Expression to Augment Cell Adhesion and Motility. Cells 14 32570949
2011 Crystallization of a paraspeckle protein PSPC1-NONO heterodimer. Acta crystallographica. Section F, Structural biology and crystallization communications 14 22102035
2021 PSPC1 regulates CHK1 phosphorylation through phase separation and participates in mouse oocyte maturation. Acta biochimica et biophysica Sinica 13 34490876
2021 Nuclear receptor 4A1 (NR4A1) antagonists target paraspeckle component 1 (PSPC1) in cancer cells. Molecular carcinogenesis 12 34699643
2023 LncRNA LOC105369504 inhibits tumor proliferation and metastasis in colorectal cancer by regulating PSPC1. Cell death discovery 11 36894530
2018 Development of PSP1, a Biostimulant Based on the Elicitor AsES for Disease Management in Monocot and Dicot Crops. Frontiers in plant science 10 30087681
2020 PSPC1: a contextual determinant of tumor progression. Molecular & cellular oncology 9 32158931
2025 PSPC1 exerts an oncogenic role in AML by regulating a leukemic transcription program in cooperation with PU.1. Cell stem cell 8 39954676
2018 PSP1, a Phosphatidylserine-Recognizing Peptide, Is Useful for Visualizing Radiation-Induced Apoptosis in Colorectal Cancer In Vitro and In Vivo. Translational oncology 8 29982102
2021 PSPC1 is a new contextual determinant of aberrant subcellular translocation of oncogenes in tumor progression. Journal of biomedical science 7 34340703
2023 PSPC1 Inhibition Synergizes with Poly(ADP-ribose) Polymerase Inhibitors in a Preclinical Model of BRCA-Mutated Breast/Ovarian Cancer. International journal of molecular sciences 5 38069409
2017 Synergistic upregulation of NONO and PSPC1 regulates Sertoli cell response to MEHP via modulation of ALDH1A1 signaling. FEBS letters 5 28117896
2023 A Putative New Role of Tv-PSP1 Recognizes IRE and ERE Hairpin Structures from Trichomonas vaginalis. Pathogens (Basel, Switzerland) 4 36678426
2013 Phosphorylations of Sds23/Psp1/Moc1 by stress-activated kinase and cAMP-dependent kinase are essential for regulating cell viability in prolonged stationary phase. Yeast (Chichester, England) 4 23640764
2024 Evaluation of PSP1 biostimulant on Fusarium graminearum-wheat pathosystem: impact on disease parameters, grain yield, and grain quality. Pest management science 3 38450978
2025 NONO, SFPQ, and PSPC1 promote telomerase recruitment to the telomere. Nature communications 2 40593584
2017 Overexpression of PSP1 enhances growth of transgenic Arabidopsis plants under ambient air conditions. Plant molecular biology 2 28455648
2025 PSPC1 knockout promotes radiosensitivity, inhibits EMT, and metastasis of nasopharyngeal carcinoma cells. Experimental cell research 1 40962170
2025 LncRNA CASC19 promotes pancreatic cancer progression by increasing PSPC1 protein stability and facilitating the oncogenic PSPC1/ β-Catenin pathway. Molecular medicine (Cambridge, Mass.) 1 41023804
2025 Regulation of the mechanoresponsive Neat1 and PSPC1 by substrate stiffness in TGF-β1-induced renal progenitor cell fate. Journal of biomedical science 1 41243096
2024 PSPC1 Binds to HCV IRES and Prevents Ribosomal Protein S5 Binding, Inhibiting Viral RNA Translation. Viruses 1 38793620
2022 Biodesulfurization of thiosulfate by a Pseudomonas strain PSP1 and the investigation of underlying metabolic mechanisms. Environmental science and pollution research international 1 35029825
2020 Promoter P -BnPSP-1 From Ramie (Boehmeria nivea L. Gaud.) Can Drive Phloem-Specific GUS Expression in Arabidopsis thaliana. Frontiers in genetics 1 33391335
2026 PSPC1-AS2/PSPC1 axis drives STAT3-dependent CCL2 expression to promote M2 macrophage polarization and liver metastasis in gastric cancer. Oncogene 0 41986651
2025 PSPC1 bridges cancer stemness and malignancy in acute myeloid leukemia. Cell stem cell 0 40054451
2025 M6A-METTL3-dependent nuclear PANC754/PSPC1/H3K4me1 repression complex regulate immune evasive LGALS7 signal to enhance immunotherapy against colorectal cancer. Cell death & disease 0 40634299
2025 PSPC1-SMAD3 axis regulates iron-induced beiging of adipocytes in white adipose tissue. Cell communication and signaling : CCS 0 41345872