Affinage

SERBP1

SERPINE1 mRNA-binding protein 1 · UniProt Q8NC51

Length
408 aa
Mass
45.0 kDa
Annotated
2026-06-10
47 papers in source corpus 26 papers cited in narrative 26 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SERBP1 is an intrinsically disordered RNA-binding protein that operates as a ribosome-associated regulator of translation and a sequence/structure-selective mRNA-stability factor coordinating DNA repair, metabolism, and cell division (PMID:30039520, PMID:34631798, PMID:26068472). Its C-terminal RGG box, together with neighboring residues flanking a non-RNA-binding central α-helix, recognizes G-rich RNA and folded G-quadruplex (G4) RNA/DNA structures by encircling the G4 in a topology-driven manner, and both RGG boxes drive RNA- and salt-dependent liquid-liquid phase separation (PMID:34631798, PMID:41846982). In situ cryo-EM places SERBP1 on the ribosome across nearly all translating and non-translating states, bridging the 60S and 40S subunits, and biochemical fractionation confirms it co-sediments with the 40S subunit and polysomes [PMID:bio_10.1101_2024.07.02.601723, PMID:30039520]. SERBP1 binds and stabilizes specific transcripts to control downstream programs: it stabilizes CtIP mRNA to license CtIP-dependent homologous recombination after DNA damage and BRCA1 mRNA to drive RAD51-mediated repair and cisplatin resistance (PMID:26068472, PMID:41856985), stabilizes GLUT2 mRNA in a SYT1-dependent protective circuit (PMID:39059605), and protects Lipt2 mRNA to suppress ferroptosis (PMID:38470932). Its activity is gated by reversible modifications: PRMT1 asymmetrically dimethylates its RG/RGG motifs to control cytoplasmic–nuclear–nucleolar partitioning and stress-granule recruitment, PKCε phosphorylates it during mitosis to repress translation, remodel 40S binding, and nucleate M-body ribonucleoprotein granules required for chromosome segregation, and serine phosphorylation in the RGG box acts as a switch lowering G4 affinity (PMID:22442049, PMID:24205981, PMID:34836941, PMID:41846982). SERBP1 partitions into stress granules and also promotes their clearance by recruiting G3BP1 and 26S proteasome subunits to drive K63-ubiquitin-dependent disassembly (PMID:24205981, PMID:37223481). Beyond cytoplasmic translation, SERBP1 acts as a scaffold linking RNA to chromatin and viral machinery—recruiting transcriptional repressors CHD3/KAP1 to the HCMV major immediate early promoter, bridging dengue virus RNA to the 40S subunit through RACK1, and forming a PCIF1 complex that deposits m6Am on target mRNAs (PMID:36504797, PMID:35266803, PMID:40764612). Loss of Serbp1 in mouse oocytes causes spindle and asymmetric-division defects and female infertility, establishing an in vivo requirement in meiotic and developmental control (PMID:40902969).

Mechanistic history

Synthesis pass · year-by-year structured walk · 25 steps
  1. 2005 Medium

    Established an early functional context by linking SERBP1/PAIRBP1 to membrane progesterone signaling, raising the question of where and how the protein acts.

    Evidence Surface immunocytochemistry, antibody blocking, and Co-IP with PGRMC1 in granulosa/luteal cells

    PMID:15814896

    Open questions at the time
    • Surface/membrane localization conflicts with later RNA-binding and ribosomal roles
    • No direct molecular mechanism linking SERBP1 to progesterone signaling defined
  2. 2006 Medium

    Mapped an early nuclear interaction network, placing SERBP1 in PML body/sumoylation and Cajal body/nucleolar contexts before its RNA functions were known.

    Evidence Yeast two-hybrid screen plus co-localization in HeLa cells (Daxx, Topors, PIAS family, TDG, HPC2)

    PMID:16679534

    Open questions at the time
    • Interactions not validated by reciprocal endogenous Co-IP
    • Functional consequence of nuclear-body partners unresolved
  3. 2012 High

    Identified PRMT1 as the enzyme that asymmetrically dimethylates SERBP1's RG/RGG motifs, answering how its subcellular distribution is controlled.

    Evidence In vitro methylation with recombinant PRMT1, siRNA knockdown, deletion mapping, immunofluorescence

    PMID:22442049

    Open questions at the time
    • Functional consequence of methylation on RNA binding not directly tested
    • Whether methylation is dynamically regulated by stimuli unknown
  4. 2013 High

    Connected methylation status to stress-granule and nucleolar targeting, defining how modification routes SERBP1 between compartments under stress.

    Evidence Immunofluorescence with stress-granule/nucleolar markers, arsenite and AdOx treatment, deletion constructs

    PMID:24205981

    Open questions at the time
    • No single domain sufficient for SG targeting; recruitment determinants incompletely defined
    • Functional role within SGs not established here
  5. 2013 Medium

    Showed SERBP1 forms a post-transcriptional regulatory RNP with SPIN1 controlling maternal transcript stability during meiosis.

    Evidence Reciprocal Co-IP with domain mapping and Spin1 conditional knockout with PDE3A mRNA readout in mouse oocytes

    PMID:23894536

    Open questions at the time
    • SERBP1-specific contribution to mRNA control partly inferred from SPIN1 phenotype
    • Direct mRNA targets of the SERBP1-SPIN1 complex not enumerated
  6. 2014 Medium

    Demonstrated SERBP1 influences proliferation and cell-cycle progression, framing it as a growth regulator.

    Evidence DNA microarray, flow-cytometry cell-cycle analysis, and siRNA/overexpression in HEK293T

    PMID:25205453

    Open questions at the time
    • Direct mRNA targets driving G1 arrest not identified
    • Transcriptional changes may be indirect
  7. 2015 High

    Provided the first direct mRNA-target mechanism: SERBP1 binds and translationally promotes CtIP in S phase, placing it upstream of homologous recombination.

    Evidence RIP-seq, polysome profiling, WT vs ΔRGG reconstitution, and CHK1/RPA2 phosphorylation after camptothecin

    PMID:26068472

    Open questions at the time
    • Whether stabilization vs translational loading is the primary mechanism not fully separated
    • RGG-dependence shown but binding mode to CtIP mRNA not structurally defined
  8. 2015 Medium

    Revealed transcriptional feedback control of SERBP1 itself by the LRH1 complex.

    Evidence Nuclear fractionation/MS, promoter:reporter assay, LRH1 knockdown/overexpression

    PMID:26398198

    Open questions at the time
    • Whether SERBP1 has reciprocal effects on LRH1 targets untested
    • Direct vs indirect promoter regulation not fully resolved
  9. 2017 Medium

    Defined a direct RACK1 interaction surface on SERBP1, providing a route to the ribosomal scaffold.

    Evidence Yeast two-hybrid with deletion and RACK1 point-mutant mapping

    PMID:28267599

    Open questions at the time
    • No reciprocal endogenous Co-IP in this study
    • Functional consequence of RACK1 binding not tested here
  10. 2018 High

    Established SERBP1 as a constitutive component of cytoplasmic 40S subunits and active polysomes, grounding its translational role biochemically.

    Evidence Subcellular fractionation, ultracentrifugation, polysome profiling, ribosome proteomics

    PMID:30039520

    Open questions at the time
    • Whether association is regulatory vs structural not resolved by fractionation alone
    • Stoichiometry on ribosomes not determined
  11. 2020 High

    Linked SERBP1 RNA binding to one-carbon metabolism and epigenetic state in cancer, broadening its role to metabolic-epigenetic control.

    Evidence siRNA knockdown, RNAcompete GC-rich motif identification, metabolomics, H3K27me3 assays, RNA-seq in GBM

    PMID:32762776

    Open questions at the time
    • Direct mRNA targets mediating methionine/one-carbon effects not pinpointed
    • Causal chain from RNA binding to H3K27me3 is indirect
  12. 2021 High

    Solved the domain architecture—intrinsically disordered with a stable central helix and RGG-driven G-rich RNA binding and phase separation—explaining how SERBP1 engages RNA and condensates.

    Evidence Solution NMR, biophysical assays, deletion analysis, LLPS assay

    PMID:34631798

    Open questions at the time
    • Function of the central helix unknown
    • Physiological RNAs driving LLPS in cells not identified
  13. 2021 High

    Identified PKCε-mediated mitotic phosphorylation as the switch that represses translation, remodels 40S binding, and nucleates M-body granules required for chromosome segregation.

    Evidence Genetically-encoded crosslinker substrate trapping, in vivo phosphorylation, knockdown with segregation/M-body readouts

    PMID:34836941

    Open questions at the time
    • Phosphosite-to-function mapping on the ribosome not fully resolved
    • Composition and assembly mechanism of M-bodies incompletely defined
  14. 2022 High

    Showed RACK1 recruits SERBP1 to bridge dengue virus RNA to the 40S subunit, demonstrating functional hijacking of its ribosomal scaffolding role.

    Evidence RACK1 interactome MS, RNAi screen, viral-RNA interaction, RACK1-binding-deficient SERBP1 mutant rescue

    PMID:35266803

    Open questions at the time
    • Whether host mRNA recruitment uses the same RACK1-dependent mechanism untested
    • Structural basis of viral RNA bridging not resolved
  15. 2022 Medium

    Extended SERBP1 to chromatin scaffolding, recruiting CHD3/KAP1 repressors to silence the HCMV MIEP during latency.

    Evidence siRNA knockdown and ChIP for CHD3/KAP1 at the MIEP in myeloid latency models

    PMID:36504797

    Open questions at the time
    • Direct DNA/chromatin binding by SERBP1 not demonstrated
    • Whether RNA bridges SERBP1 to the promoter unknown
  16. 2022 Medium

    Placed SERBP1 as a modulator of Ago2-RISC activity on specific 3'UTR targets in neurons.

    Evidence IP/LC-MS/MS, RIP for KCC2 3'UTR, siRNA, luciferase reporter

    PMID:35326503

    Open questions at the time
    • Mechanism of Ago2 modulation (recruitment vs displacement) unresolved
    • Direct vs indirect interaction with RISC not separated
  17. 2023 High

    Revealed SERBP1 as a driver of stress-granule clearance by recruiting G3BP1 and proteasome subunits to enable ubiquitin-dependent disassembly, with an in vivo germ-cell protective role.

    Evidence Co-IP, proteasome activity and K63-ubiquitination assays, knockdown in somatic/germ cells, scrotal heat-stress model

    PMID:37223481

    Open questions at the time
    • How SERBP1 reconciles SG recruitment with SG clearance not fully resolved
    • Direct vs scaffold-mediated proteasome recruitment unclear
  18. 2024 Medium

    Showed acetylation governs SERBP1's mRNA-protective function, with SIRT3 deacetylation derepressing Lipt2 degradation and modulating ferroptosis in a viral context.

    Evidence Acetylation proteomics, SIRT3 deacetylation assay, Lipt2 RIP/stability, pharmacological/genetic perturbation, transformation assay

    PMID:38470932

    Open questions at the time
    • Specific acetyl-lysine residues controlling RNA binding not mapped
    • Generality beyond Lipt2 untested
  19. 2024 Medium

    Linked SERBP1 to GLUT2 mRNA stabilization via SYT1, defining a protective metabolic circuit in renal cells.

    Evidence IP-shotgun proteomics, SERBP1 RNAi, GLUT2 mRNA stability and toxicity assays

    PMID:39059605

    Open questions at the time
    • Mechanism by which SYT1 binding stabilizes SERBP1 unknown
    • Direct SERBP1-GLUT2 mRNA contact not structurally defined
  20. 2024 Medium

    Captured SERBP1 in situ on the ribosome across nearly all functional states, bridging 60S and 40S at sites invisible on purified ribosomes.

    Evidence In situ single-particle cryo-EM (cryo-FIB), 2.19 Å consensus 80S structure, 21 states (preprint)

    PMID:bio_10.1101_2024.07.02.601723

    Open questions at the time
    • Regulatory function inferred from structural occupancy, not functionally tested
    • Preprint, awaits peer review
  21. 2025 Medium

    Defined the structural basis of G-quadruplex recognition by the RGG box and identified serine phosphorylation as a binding switch, with mTOR 5'UTR G4 as a functional target.

    Evidence NMR, biophysical binding, MD/docking, phosphomimetic mutagenesis, knockdown with mTOR readout (preprint)

    PMID:41846982

    Open questions at the time
    • Preprint, awaits peer review
    • Which kinase phosphorylates the regulatory serines in vivo unknown
  22. 2025 Medium

    Showed SERBP1 partners with PARP1/PARylation machinery and G4-binding proteins and appears in pathological aggregates, broadening its interactome to splicing, division, and ribosome biogenesis.

    Evidence Interactome Co-IP/MS, PARylation assays, G4-partner enrichment, Alzheimer's brain tissue analysis

    PMID:39937575

    Open questions at the time
    • Direct vs PAR-mediated nature of many interactions unresolved
    • Causal role in disease aggregates not established
  23. 2025 High

    Established a SERBP1-PCIF1 complex that deposits m6Am on mRNA in vivo, linking SERBP1 to RNA modification and behavior.

    Evidence Co-IP, m6Am mapping, virus-mediated neuronal gain/loss-of-function, behavioral assays

    PMID:40764612

    Open questions at the time
    • Whether SERBP1 confers target specificity to PCIF1 mechanistically unclear
    • Generality of SERBP1-dependent m6Am beyond Maf1 untested
  24. 2025 Medium

    Demonstrated SERBP1 stabilizes BRCA1 mRNA to drive RAD51-mediated HR and chemoresistance, extending its DNA-repair role to a SERBP1-BRCA1-RAD51 axis.

    Evidence Gain/loss-of-function, BRCA1 mRNA stability, RAD51 foci, in vitro/in vivo cisplatin resistance with BRCA1 rescue

    PMID:41856985

    Open questions at the time
    • Direct SERBP1-BRCA1 mRNA binding not structurally shown
    • Relationship to the earlier CtIP-HR axis not integrated
  25. 2025 High

    Provided an in vivo organismal requirement: oocyte-specific Serbp1 loss causes spindle/asymmetric-division defects and female infertility with germline-somatic crosstalk.

    Evidence Conditional knockout mouse, spindle imaging, granulosa apoptosis, Erk1/2 phosphorylation

    PMID:40902969

    Open questions at the time
    • Molecular targets mediating spindle defects not identified
    • Whether phenotype reflects translational vs mRNA-stability functions unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how SERBP1's many modification states (methylation, phosphorylation, acetylation) integrate on the ribosome to switch between promoting translation, repressing it, and selectively stabilizing specific mRNAs.
  • No unified model coupling modification state to ribosome occupancy and target mRNA selection
  • Genome-wide direct mRNA target map versus ribosome-structural role not reconciled
  • Causal direction between SERBP1's translational and chromatin/RNA-modification roles unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 4 GO:0045182 translation regulator activity 3 GO:0060090 molecular adaptor activity 3 GO:0098772 molecular function regulator activity 3 GO:0003677 DNA binding 1
Localization
GO:0005829 cytosol 3 GO:0005634 nucleus 2 GO:0005730 nucleolus 2 GO:0005840 ribosome 2
Pathway
R-HSA-1640170 Cell Cycle 3 R-HSA-1643685 Disease 3 R-HSA-392499 Metabolism of proteins 3 R-HSA-8953854 Metabolism of RNA 3 R-HSA-73894 DNA Repair 2 R-HSA-8953897 Cellular responses to stimuli 2
Partners
G3BP1PARP1PCIF1PGRMC1PKCEPSILONPRMT1RACK1SPIN1
Complex memberships
40S ribosomal subunit / 80S ribosomeLRH1 transcriptional complexM-body ribonucleoprotein granuleSERBP1-PCIF1 m6Am methyltransferase complex

Evidence

Reading pass · 26 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2012 SERBP1 is asymmetrically dimethylated at arginine residues in its middle RG and C-terminal RGG regions by PRMT1. Knockdown of PRMT1 significantly reduced aDMA levels on SERBP1, and recombinant PRMT1 directly methylated SERBP1 in vitro. This methylation regulates subcellular localization: hypomethylation (via AdOx treatment or PRMT1 siRNA) shifts SERBP1 from predominantly cytoplasmic to nuclear localization. Co-immunoprecipitation, in vitro methylation assay with recombinant PRMT1, siRNA knockdown, immunofluorescence, deletion construct analysis Journal of cellular biochemistry High 22442049
2013 Under normal conditions SERBP1 localizes predominantly in the cytoplasm; upon arsenite-induced stress, a proportion co-localizes with stress granule marker TIA-1 in cytoplasmic stress granules, while another pool redistributes to the nucleolus. Hypomethylation (AdOx treatment) retains SERBP1 in the nucleus/nucleolus regardless of stress. Arginine methylation status is required for efficient recruitment to and retention in stress granules; all three SERBP1 domains contribute to stress granule targeting but none alone is sufficient. Immunofluorescence with stress granule markers, arsenite stress treatment, adenosine periodate (methylation inhibitor) treatment, truncation/deletion constructs, fluorescence microscopy The FEBS journal High 24205981
2006 CGI-55 (SERBP1) interacts with Daxx, Topors, PIAS1, PIAS3, PIASy, UBA2, TDG, and HPC2 — proteins associated with PML nuclear bodies, sumoylation, and transcriptional regulation — as identified by yeast two-hybrid and confirmed by co-localization in HeLa cells. SERBP1 localizes to the nucleolus and co-localizes with p80-coilin-positive nuclear Cajal bodies. Yeast two-hybrid screen, in vivo co-localization with GFP/RFP fusion proteins, domain mapping Cell biochemistry and biophysics Medium 16679534
2015 SERBP1 regulates CtIP expression at the translational level specifically in S phase. SERBP1 binds CtIP mRNA (identified by RIP-seq), and SERBP1 depletion reduces polysome-associated CtIP mRNA and CtIP protein levels in S phase. Reconstitution with wild-type SERBP1 but not an RNA-binding-defective ΔRGG mutant rescues CtIP expression. SERBP1 depletion abrogates CHK1 and RPA2 phosphorylation (HR activation markers) after camptothecin-induced DSBs, placing SERBP1 upstream of CtIP-mediated homologous recombination. RIP-seq, siRNA knockdown, polysome profiling, reconstitution with WT and ΔRGG mutant, phosphorylation assays (CHK1, RPA2) Nucleic acids research High 26068472
2018 Mammalian SERBP1 associates with cytoplasmic ribosomes as a component of the 40S small subunit and is present in actively translating polysomes. Subcellular fractionation showed cytoplasmic SERBP1 is pelleted by ultracentrifugation; cosedimentation with the 40S subunit was confirmed after ribosomal subunit dissociation; SERBP1 was identified by proteomic analysis in rodent testis ribosomes and in human cancer cell ribosomes. Subcellular fractionation, ultracentrifugation, polysome profiling, proteomic/mass spectrometry analysis, cosedimentation assay Cell biochemistry and function High 30039520
2017 SERBP1 interacts selectively with the scaffold protein RACK1 via its C-terminal third (which contains one of its two PRMT1 substrate sites). Multiple SERBP1 isoforms interact with RACK1 with indistinguishable affinity. Single amino acid substitutions in RACK1 that disrupt SERBP1 binding substantially overlap with those disrupting PDE4D5 binding, indicating a shared interaction surface. Yeast two-hybrid system with beta-galactosidase assay, deletion construct analysis, reverse two-hybrid screen with RACK1 point mutants Cellular signalling Medium 28267599
2021 SERBP1 is a substrate of PKCε: PKCε phosphorylates SERBP1 during mitosis, repressing protein translation and altering SERBP1 binding to the 40S ribosomal subunit. This promotes the assembly of ribonucleoprotein granules (M-bodies) containing SERBP1. SERBP1 is necessary for chromosome segregation and successful cell division independently of Aurora B, and M-body formation correlates with this requirement. UV-photocrosslinkable amino acid genetically-encoded crosslinker screen, in vivo phosphorylation assay, SERBP1 knockdown with chromosome segregation readout, ribosome association assay, M-body imaging Nature communications High 34836941
2021 SERBP1 is an intrinsically disordered protein containing a stable central α-helix; it binds G-rich RNA sequences through its C-terminal RGG box and neighboring residues. Both RGG boxes are required for efficient liquid-liquid phase separation (LLPS) mediated by salt and RNA. The central helix does not participate in RNA binding and the RGG boxes do not stabilize the central helix. Solution NMR spectroscopy, biophysical assays (multiple techniques), deletion/domain analysis, LLPS assay Frontiers in molecular biosciences High 34631798
2013 SPINDLIN1 (SPIN1), via its Tudor-like domain, forms a ribonucleoprotein complex with SERBP1 in mouse oocytes. This complex is involved in regulating mRNA stability and/or translation. Loss of Spin1 reduces PDE3A mRNA levels and causes meiotic arrest, placing SERBP1-SPIN1 interaction in the post-transcriptional control of maternal transcripts required for meiotic resumption. Co-immunoprecipitation, domain deletion analysis, conditional knockout mouse model, RNA level analysis PloS one Medium 23894536
2020 SERBP1 knockdown in GBM cells decreases methionine production, causing a reduction in histone H3K27me3 methylation and upregulation of neurogenesis/differentiation genes. SERBP1 regulates metabolic routes (one-carbon metabolism) used preferentially by cancer cells, indirectly modulating epigenetic regulation. SERBP1 binds GC-rich RNA motifs as identified by RNAcompete. siRNA knockdown, RNAcompete motif identification, metabolomics (methionine levels), histone methylation assays (H3K27me3), RNA-seq, GBM and glioma stem cell functional assays Genome biology High 32762776
2022 RACK1, as part of the dengue virus (DENV) replication complex on the 40S ribosomal subunit, recruits SERBP1 (and Vigilin). SERBP1 interacts with the DENV RNA genome and its genetic ablation reduces viral translation and replication. A SERBP1 mutant lacking RACK1 binding but retaining viral RNA interaction cannot support DENV infection, indicating RACK1-SERBP1 interaction is required to link DENV RNA to the translation machinery. Mass spectrometry RACK1 interactome, RNA interference screen, genetic ablation, RNA-protein interaction assay with viral genome, SERBP1 RACK1-binding mutant analysis Journal of virology High 35266803
2022 SERBP1 is upregulated during HCMV latency and functions as a scaffold protein to recruit the transcriptional repressor CHD3 (and KAP1) to the viral major immediate early promoter (MIEP), mediating epigenetic silencing during latent infection of myeloid cells. SERBP1 is required for MIEP suppression during latency. siRNA knockdown of SERBP1, ChIP assay for CHD3 and KAP1 at the MIEP, latency model in myeloid/CD34+ cells Frontiers in microbiology Medium 36504797
2022 SERBP1 associates with Argonaute2 (Ago2) in neuronal cells and modulates miRNA-mediated silencing. SERBP1 silencing attenuates miR-92-mediated repression of KCC2 3'UTR. Both SERBP1 and the Ago2/miR-92 complex bind to the KCC2 3'UTR, placing SERBP1 as a modulator of Ago2-RISC activity on this target. Immunoprecipitation and LC-MS/MS identification of Ago2 partners, RIP assay for KCC2 3'UTR binding, siRNA knockdown of SERBP1, luciferase reporter assay with KCC2 3'UTR Cells Medium 35326503
2023 SERBP1 promotes stress granule (SG) clearance by interacting with the SG core component G3BP1 and 26S proteasome subunits PSMD10 and PSMA3, recruiting them to SGs. SERBP1 depletion results in reduced 20S proteasome activity at SGs, mislocalized VCP and FAF2, and diminished K63-linked polyubiquitination of G3BP1 during SG recovery. In vivo, SERBP1 depletion in testicular cells increases germ cell apoptosis upon heat stress. Co-immunoprecipitation, proteasome activity assay, ubiquitination assay (K63-linked), siRNA knockdown in somatic and germ cells, in vivo scrotal heat stress model Research (Washington, D.C.) High 37223481
2024 KSHV-encoded vIL-6 promotes SIRT3-mediated deacetylation of SERBP1. Deacetylated SERBP1 fails to bind and protect Lipt2 mRNA from degradation, resulting in Lipt2 mRNA destabilization and ferroptosis suppression required for KSHV-induced cellular transformation. Acetylation of SERBP1 is thus a regulatory switch governing its mRNA-protective function on Lipt2 transcripts. Acetylation proteomics, SERBP1 deacetylation assay with SIRT3, RIP/mRNA stability assay for Lipt2, siRNA knockdown, SIRT3 inhibitor (3-TYP) treatment, cellular transformation assay PLoS pathogens Medium 38470932
2015 SERBP1 is a component of the liver receptor homologue-1 (LRH1) transcriptional complex, identified by nuclear fractionation and mass spectrometry. LRH1 binds the SERBP1 promoter and represses its transcription; LRH1 knockdown increases SERBP1 expression, while LRH1 overexpression decreases SERBP1 mRNA levels. Nuclear fractionation, mass spectrometry, Western blot co-purification, siRNA knockdown of LRH1, promoter:reporter assay Journal of proteome research Medium 26398198
2025 SERBP1 interacts with PARP1 and its associated factors, influences PARylation activity, and participates in protein complexes that are predominantly PARylated or contain PAR binders. SERBP1 preferentially interacts with G-quadruplex (G4)-binding proteins. SERBP1 is present in pathological stress granules and Tau aggregates in Alzheimer's brains, and has roles in splicing, cell division, and ribosome biogenesis as defined by interactome analysis. Interactome/proteomics (Co-IP + MS), PARylation assay, G4-binding partner enrichment analysis, patient brain tissue analysis eLife Medium 39937575
2024 In situ cryo-EM revealed that SERBP1 binds to the ribosome in almost all translating and non-translating states inside human cells, bridging the 60S and 40S ribosomal subunits at newly identified binding sites not observed on purified ribosomes, suggesting SERBP1 plays an important regulatory role in translation. In situ single-particle cryo-EM (cryo-FIB milling + in situ cryo-EM), 2.19 Å consensus structure of 80S ribosome, 21 functional states resolved bioRxivpreprint Medium bio_10.1101_2024.07.02.601723
2025 SERBP1 recognizes G-quadruplex (G4) RNA and DNA structures with low micromolar affinity through its RGG box, which wraps around the G4 (encircling mechanism). C-terminal serine residues stabilize the complex through hydrogen bonding; phosphomimetic mutations of these serines reduce binding affinity, identifying phosphorylation as a regulatory switch. Recognition is driven by G4 topology rather than sequence. SERBP1 depletion reduces mTOR expression in glioblastoma cells via G4 elements in the mTOR 5' UTR. NMR spectroscopy, biophysical binding assays, molecular dynamics and docking simulations, phosphomimetic mutagenesis, SERBP1 knockdown with mTOR expression readout bioRxivpreprint Medium 41846982
2005 PAIRBP1 (SERBP1) is present on the extracellular surface of granulosa and luteal cells, and an antibody against PAIRBP1 attenuates progesterone's antiapoptotic action in these cells without reducing progesterone binding. PAIRBP1 co-immunoprecipitates with the membrane progesterone binding protein PGRMC1, suggesting SERBP1 mediates progesterone's antiapoptotic signaling through interaction with PGRMC1. Immunocytochemistry on living non-permeabilized cells, antibody blocking assay, immunoprecipitation with PGRMC1, radiolabeled progesterone binding assay Biology of reproduction Medium 15814896
2025 SERBP1 forms a complex with PCIF1 (a methyltransferase) and this complex mediates m6Am deposition onto mRNA in glutamatergic neurons of the primary somatosensory cortex. SERBP1-PCIF1 upregulation in these neurons adds m6Am onto Maf1 mRNA, reducing MAF1 protein and contributing to neuropathic pain and anxiety comorbidity. Blocking SERBP1-PCIF1 upregulation abolishes m6Am gain on Maf1 and elevates MAF1 protein. Co-immunoprecipitation (SERBP1-PCIF1 complex), m6Am sequencing/detection, conditional neuronal manipulation (virus-mediated), behavioral assays for neuropathic pain and anxiety Nature communications High 40764612
2025 SERBP1 promotes cisplatin resistance in lung adenocarcinoma by stabilizing BRCA1 mRNA, thereby activating RAD51-mediated homologous recombination repair. BRCA1 knockdown attenuates SERBP1-driven cisplatin resistance both in vitro and in vivo, establishing BRCA1 as a critical downstream effector in a SERBP1-BRCA1-RAD51 axis. siRNA/shRNA gain- and loss-of-function experiments, mRNA stability assay for BRCA1, RAD51 focus formation assay, in vitro and in vivo cisplatin resistance assays Cell death discovery Medium 41856985
2025 Cryo-EM revealed SERBP1 in an eEF2/SERBP1-associated dormant ribosome state that accumulates upon treatment with the translation inhibitor NT-2 mycotoxin, confirming SERBP1 association with an inactive ribosomal state in human cells. Cryo-EM at 1.76 Å resolution of human 80S ribosome from cell-free lysate treated with NT-2 bioRxivpreprint Low bio_10.1101_2025.10.11.680285
2014 CGI-55 (SERBP1) overexpression in HEK293T cells reduces cell proliferation mainly through G1 phase arrest; siRNA knockdown of CGI-55/SERBP1 causes an increase in proliferation. SERBP1 overexpression downregulates genes associated with proliferation, apoptosis, and cell cycle control. DNA microarray transcriptomics after overexpression/siRNA knockdown, flow cytometry cell cycle analysis, qRT-PCR validation Biochimica et biophysica acta Medium 25205453
2024 SYT1 (Synaptotagmin-1) binds to and stabilizes SERBP1 protein, and SERBP1 in turn enhances the stability of GLUT2 mRNA and its protein levels, protecting renal cells from paraquat intracellular accumulation. Immunoprecipitation-shotgun identified SERBP1 as a SYT1-bound protein; RNA interference of SERBP1 abolished SYT1's protective effects. Immunoprecipitation-shotgun proteomics, RNA interference of SERBP1, mRNA stability assay for GLUT2, cell toxicity and intracellular PQ accumulation assays Chemico-biological interactions Medium 39059605
2025 Conditional deletion of Serbp1 in mouse oocytes (using Zp3/Gdf9-Cre) results in arrested oocyte growth, spindle assembly defects, impaired asymmetric cell division, failure of blastocyst formation, and female infertility. Serbp1 loss also induces granulosa cell apoptosis and elevated Erk1/2 phosphorylation, indicating both cell-autonomous and somatic-germline crosstalk functions. Conditional knockout mouse (Cre-lox), oocyte phenotype analysis (spindle imaging, meiotic competence), granulosa cell apoptosis assay, Erk1/2 phosphorylation assay Molecular and cellular endocrinology High 40902969

Source papers

Stage 0 corpus · 47 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2020 The RNA-binding protein SERBP1 functions as a novel oncogenic factor in glioblastoma by bridging cancer metabolism and epigenetic regulation. Genome biology 83 32762776
2005 Expression and function of PAIRBP1 within gonadotropin-primed immature rat ovaries: PAIRBP1 regulation of granulosa and luteal cell viability. Biology of reproduction 68 15814896
2017 MiR-218 suppresses the metastasis and EMT of HCC cells via targeting SERBP1. Acta biochimica et biophysica Sinica 61 28369267
2007 Expression analysis and RNA localization of PAI-RBP1 (SERBP1) in epithelial ovarian cancer: association with tumor progression. Gynecologic oncology 47 17698176
2013 Localization of SERBP1 in stress granules and nucleoli. The FEBS journal 45 24205981
2012 Protein arginine methylation of SERBP1 by protein arginine methyltransferase 1 affects cytoplasmic/nuclear distribution. Journal of cellular biochemistry 43 22442049
2013 Expression of progesterone receptor membrane component (PGRMC) 1 and 2, serpine mRNA binding protein 1 (SERBP1) and nuclear progesterone receptor (PGR) in the bovine endometrium during the estrous cycle and the first trimester of pregnancy. Reproductive biology 40 23522067
2016 Loss of miR-26a-5p promotes proliferation, migration, and invasion in prostate cancer through negatively regulating SERBP1. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 39 27449037
2015 SERBP1 affects homologous recombination-mediated DNA repair by regulation of CtIP translation during S phase. Nucleic acids research 36 26068472
2018 The mRNA-binding protein Serbp1 as an auxiliary protein associated with mammalian cytoplasmic ribosomes. Cell biochemistry and function 34 30039520
2022 RACK1 Associates with RNA-Binding Proteins Vigilin and SERBP1 to Facilitate Dengue Virus Replication. Journal of virology 29 35266803
2021 Structural Characterization of the RNA-Binding Protein SERBP1 Reveals Intrinsic Disorder and Atypical RNA Binding Modes. Frontiers in molecular biosciences 28 34631798
2013 A tudor domain protein SPINDLIN1 interacts with the mRNA-binding protein SERBP1 and is involved in mouse oocyte meiotic resumption. PloS one 28 23894536
2006 CGI-55 interacts with nuclear proteins and co-localizes to p80-coilin positive-coiled bodies in the nucleus. Cell biochemistry and biophysics 28 16679534
2022 SIX5-activated LINC01468 promotes lung adenocarcinoma progression by recruiting SERBP1 to regulate SERPINE1 mRNA stability and recruiting USP5 to facilitate PAI1 protein deubiquitylation. Cell death & disease 23 35387981
2017 Dynamic expression of PGRMC1 and SERBP1 in human endometrium: an implication in the human decidualization process. Fertility and sterility 23 28911927
2023 SERBP1 Promotes Stress Granule Clearance by Regulating 26S Proteasome Activity and G3BP1 Ubiquitination and Protects Male Germ Cells from Thermostimuli Damage. Research (Washington, D.C.) 21 37223481
2012 Differential expression of PAI-RBP1, C1orf142, and COTL1 in non-small cell lung cancer cell lines with different tumor metastatic potential. Journal of investigative medicine : the official publication of the American Federation for Clinical Research 21 22373659
2021 CircRNA circBACH1 (hsa_circ_0061395) serves as a miR-656-3p sponge to facilitate hepatocellular carcinoma progression through increasing SERBP1 expression. Biochemical and biophysical research communications 20 33831787
2021 A genetically-encoded crosslinker screen identifies SERBP1 as a PKCε substrate influencing translation and cell division. Nature communications 20 34836941
2017 The RNA-binding protein SERBP1 interacts selectively with the signaling protein RACK1. Cellular signalling 20 28267599
2020 lncRNA TMPO-AS1 Exerts Oncogenic Roles in HCC Through Regulating miR-320a/SERBP1 Axis. OncoTargets and therapy 18 32753892
2021 miR-362-3p acts as a tumor suppressor by targeting SERBP1 in ovarian cancer. Journal of ovarian research 17 33526047
2014 Ki-1/57 and CGI-55 ectopic expression impact cellular pathways involved in proliferation and stress response regulation. Biochimica et biophysica acta 17 25205453
2024 KSHV vIL-6 promotes SIRT3-induced deacetylation of SERBP1 to inhibit ferroptosis and enhance cellular transformation by inducing lipoyltransferase 2 mRNA degradation. PLoS pathogens 14 38470932
2019 Complex interactomes and post-translational modifications of the regulatory proteins HABP4 and SERBP1 suggest pleiotropic cellular functions. World journal of biological chemistry 13 31768228
2016 Expression of Progesterone Receptor Membrane Component 1 (PGRMC1), Progestin and AdipoQ Receptor 7 (PAQPR7), and Plasminogen Activator Inhibitor 1 RNA-Binding Protein (PAIRBP1) in Glioma Spheroids In Vitro. BioMed research international 13 27340667
2023 miR-145 Modulates Fatty Acid Metabolism by Targeting FOXO1 to Affect SERBP1 Activity in Bovine Mammary Epithelial Cells. Journal of agricultural and food chemistry 11 37154263
2022 Latency-associated upregulation of SERBP1 is important for the recruitment of transcriptional repressors to the viral major immediate early promoter of human cytomegalovirus during latent carriage. Frontiers in microbiology 11 36504797
2022 Silencing of Ago-2 Interacting Protein SERBP1 Relieves KCC2 Repression by miR-92 in Neurons. Cells 8 35326503
2022 SERBP1 affects the apoptotic level by regulating the expression and alternative splicing of cellular and metabolic process genes in HeLa cells. PeerJ 8 36213507
2021 Circ_0046600 promotes hepatocellular carcinoma progression via up-regulating SERBP1 through sequestering miR-1258. Pathology, research and practice 7 34784519
2015 SERBP1 Is a Component of the Liver Receptor Homologue-1 Transcriptional Complex. Journal of proteome research 7 26398198
2021 The 1H, 15N and 13C resonance assignments of the C-terminal domain of Serpine mRNA binding protein 1 (SERBP1). Biomolecular NMR assignments 5 34436734
2025 SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis. eLife 4 39937575
2025 The 1H, 15N and 13C backbone resonance assignments of the N-terminal (1-149) domain of Serpine mRNA Binding Protein 1 (SERBP1). Biomolecular NMR assignments 3 40153110
2025 SERBP1-PCIF1 complex-controlled m6Am modification in glutamatergic neurons of the primary somatosensory cortex is required for neuropathic pain in mice. Nature communications 3 40764612
2024 Avian leukosis virus usurps the cellular SERBP1 protein to enhance its transcription and promote productive infections in avian cells. Poultry science 3 38663206
2025 "SERBP1 (Hero45) is a Novel Link with Ischemic Heart Disease Risk: Associations with Coronary Arteries Occlusion, Blood Coagulation and Lipid Profile". Cell biochemistry and biophysics 2 40175693
2025 Clinical and immunohistochemical effects of OncoTherad (MRB-CFI-1) nanoimmunotherapy on SERBP1, HABP4, CD44 and Ki-67 in BCG-unresponsive non-muscle invasive bladder cancer. Tissue & cell 1 39938427
2025 RNA binding protein SERBP1 is indispensable for oocyte development and maturation in mice. Molecular and cellular endocrinology 1 40902969
2024 SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis. bioRxiv : the preprint server for biology 1 38585848
2026 Intrinsically disordered SERBP1 regulates translation through topology-driven G-quadruplex recognition. bioRxiv : the preprint server for biology 0 41846982
2026 SERBP1 is required for efficient HR repair and cisplatin chemoresistance in lung adenocarcinoma. Cell death discovery 0 41856985
2025 Dual molecular axis of resistance and immunoresponsiveness to BCG in pT1 non-muscle invasive bladder cancer: Insights from HER-2, SERBP1, HABP4, and IFN-γ profiling. Tissue & cell 0 40967126
2025 Super-enhancer-driven ELOVL5 promotes T-ALL progression through the MYC-SERBP1 pathway. Genomics 0 41016515
2024 Synaptotagmin-1 antagonizes paraquat intracellular accumulation and nephrocyte toxicity by up-regulating SERBP1/GLUT2 expression. Chemico-biological interactions 0 39059605

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