| 2012 |
SERBP1 is asymmetrically dimethylated on arginines in its RG and RGG regions by PRMT1; this arginine methylation regulates cytoplasmic/nuclear distribution, with hypomethylation causing nuclear/nucleolar retention. |
Co-immunoprecipitation of endogenous PRMT1 with SERBP1, recombinant PRMT1 in vitro methylation assay, PRMT1 siRNA knockdown reducing aDMA levels, immunofluorescence of deletion constructs with AdOx treatment |
Journal of cellular biochemistry |
High |
22442049
|
| 2013 |
Under normal conditions, SERBP1 interacts with arginine-methylated and stress granule-associated proteins (hnRNP A1, FMRP, FXR1) in an RNA-dependent manner; upon arsenite stress, a proportion of SERBP1 co-localizes with TIA-1-positive cytoplasmic stress granules while another fraction concentrates in the nucleolus. Hypomethylation (via AdOx) retains SERBP1 in the nucleus/nucleolus and delays its association/dissociation with stress granules. |
Co-immunoprecipitation, immunofluorescence with deletion constructs, arsenite and AdOx treatment, co-localization with TIA-1 stress granule marker |
The FEBS journal |
High |
24205981
|
| 2015 |
SERBP1 binds CtIP mRNA during S phase and promotes its translation, thereby regulating CtIP protein levels required for homologous recombination-mediated DNA repair after double-strand breaks. An RNA-binding defective mutant (SERBP1 ΔRGG) fails to rescue CtIP expression. |
RNA immunoprecipitation-coupled RNA sequencing (RIP-seq), polysome profiling, SERBP1 knockdown with rescue using wild-type vs. ΔRGG mutant, CHK1 and RPA2 phosphorylation as HR readouts |
Nucleic acids research |
High |
26068472
|
| 2017 |
SERBP1 interacts selectively with RACK1 via its C-terminal third (which contains one PRMT1 substrate site); this interaction surface on RACK1 substantially overlaps with the binding site for PDE4D5. |
Yeast two-hybrid screen, beta-galactosidase interaction assay with SERBP1 isoforms and deletion constructs, reverse two-hybrid screen with RACK1 point mutants |
Cellular signalling |
Medium |
28267599
|
| 2018 |
Mammalian SERBP1 localizes to the nucleolus and cytoplasm; cytoplasmic SERBP1 pellets by ultracentrifugation and is identified by proteomic analysis as a component of the 40S ribosomal subunit that co-sediments with polysomes (translating ribosomes). |
Subcellular fractionation, ultracentrifugation, mass spectrometry of rodent testis ribosomes, polysome profiling with cosedimentation after subunit dissociation |
Cell biochemistry and function |
High |
30039520
|
| 2020 |
SERBP1 binds GC-rich RNA motifs and regulates metabolic gene networks in glioblastoma, including genes controlling methionine production; SERBP1 knockdown reduces methionine levels and consequently decreases H3K27me3 histone methylation, upregulating neurogenesis/differentiation genes. |
RNAcompete binding motif identification, SERBP1 knockdown in GBM and glioma stem cell lines, metabolomics, ChIP-seq for H3K27me3, RNA-seq |
Genome biology |
High |
32762776
|
| 2021 |
SERBP1 is a substrate of PKCε; PKCε phosphorylation of SERBP1 represses protein translation, alters SERBP1 binding to the 40S ribosomal subunit, and promotes assembly of ribonucleoprotein granules (M-bodies) during mitosis. SERBP1 is required for chromosome segregation and successful cell division independently of Aurora B. |
UV-photocrosslinkable amino acid trapping in PKCε kinase domain (genetically encoded crosslinker screen), validation of SERBP1 as PKCε substrate, ribosome binding assays, live imaging of M-body formation, SERBP1 KD with chromosome segregation readout |
Nature communications |
High |
34836941
|
| 2021 |
SERBP1 is an intrinsically disordered protein that lacks canonical RNA-binding motifs; it preferentially binds G-rich RNA sequences via its C-terminal RGG box and neighboring residues. SERBP1 undergoes liquid-liquid phase separation mediated by salt and RNA, requiring both RGG boxes for efficient condensate formation. |
Solution NMR, biophysical binding assays, truncation analysis, LLPS assay |
Frontiers in molecular biosciences |
High |
34631798
|
| 2022 |
SERBP1 associates with RACK1 and the dengue virus (DENV) RNA genome and facilitates DENV replication by linking the viral RNA to the translation machinery at the 40S ribosomal subunit; a SERBP1 mutant lacking RACK1 binding but retaining viral RNA interaction is unable to support DENV infection. |
RACK1 interactome mass spectrometry, RNA interference screen, genetic ablation of SERBP1, SERBP1 mutant lacking RACK1 binding domain, viral translation/replication assays |
Journal of virology |
High |
35266803
|
| 2022 |
SERBP1 interacts with Argonaute2 (Ago2) and is present in the RISC complex; SERBP1 silencing attenuates miR-92-mediated repression of the KCC2 3'UTR in neuronal cells, indicating SERBP1 modulates miRNA-dependent translational repression. |
Co-immunoprecipitation of Ago2 followed by LC-MS/MS identification of SERBP1, RIP demonstrating SERBP1 and Ago2/miR-92 binding to KCC2 3'UTR, SERBP1 siRNA knockdown with luciferase reporter assays |
Cells |
Medium |
35326503
|
| 2022 |
SERBP1 is upregulated during HCMV latency and functions as a scaffold protein to recruit transcriptional repressors CHD3 and KAP1 to the viral major immediate early promoter (MIEP), mediating epigenetic silencing of the MIEP during latent infection. |
siRNA knockdown of SERBP1 in latently infected myeloid cells, ChIP assay for CHD3 and KAP1 at the MIEP, quantitative RT-PCR for MIEP activity |
Frontiers in microbiology |
Medium |
36504797
|
| 2023 |
SERBP1 promotes stress granule (SG) clearance by interacting with the SG core component G3BP1 and 26S proteasome proteins (PSMD10 and PSMA3), recruiting them to SGs; SERBP1 absence reduces 20S proteasome activity, mislocalizes VCP/FAF2, and diminishes K63-linked polyubiquitination of G3BP1 during SG disassembly. SERBP1 depletion in testicular cells increases germ cell apoptosis upon heat stress. |
Co-immunoprecipitation of SERBP1 with G3BP1, PSMD10, PSMA3; proteasome activity assay; ubiquitination assay; SERBP1 KO in testicular cells with heat stress phenotype |
Research (Washington, D.C.) |
High |
37223481
|
| 2024 |
KSHV-encoded vIL-6 promotes SIRT3-mediated deacetylation of SERBP1; when deacetylated, SERBP1 fails to bind and protect Lipt2 mRNA from degradation, leading to ferroptosis suppression and enhanced KSHV-induced cellular transformation. |
Acetylation proteomics, SIRT3 inhibitor (3-TYP) treatment, SERBP1 deacetylation assay, mRNA stability assay for Lipt2, ferroptosis assays, cellular transformation assays |
PLoS pathogens |
Medium |
38470932
|
| 2025 |
SERBP1 interacts with PARP1 and participates in PARylation-dependent protein complexes; SERBP1 influences PARylation levels, while PARylation in turn modulates SERBP1 function and complex membership. SERBP1 preferentially interacts with G-quadruplex (G4)-binding proteins across multiple stages of gene expression and is present in Tau aggregates in Alzheimer's brains. |
Interactome mapping (AP-MS), PARylation assays, G4-binding partner analysis, immunofluorescence in Alzheimer's brain tissue, splicing and ribosome biogenesis functional assays |
eLife |
Medium |
39937575
|
| 2025 |
SERBP1 forms a complex with PCIF1 that mediates m6Am mRNA modification; in glutamatergic neurons of the primary somatosensory cortex, the SERBP1-PCIF1 complex deposits m6Am on Maf1 mRNA, reducing MAF1 protein levels and contributing to neuropathic pain and anxiety. |
Co-immunoprecipitation of SERBP1-PCIF1 complex, m6Am-seq to map modification sites, conditional knockdown in specific neuron populations, behavioral assays for neuropathic pain/anxiety, viral vector-mediated expression |
Nature communications |
High |
40764612
|
| 2025 |
SERBP1 stabilizes BRCA1 mRNA, thereby activating RAD51-mediated homologous recombination repair; this SERBP1-BRCA1 axis confers cisplatin resistance in lung adenocarcinoma, and BRCA1 knockdown abrogates SERBP1-driven resistance both in vitro and in vivo. |
Gain/loss-of-function experiments, mRNA stability assay for BRCA1, RAD51 foci assay, BRCA1 KD epistasis in xenograft model |
Cell death discovery |
Medium |
41856985
|
| 2006 |
CGI-55 (SERBP1) interacts with Daxx, Topors, PIASy, UBA2, TDG, and PIAS1/3 in the nucleus and co-localizes with p80-coilin-positive nuclear Cajal bodies and the nucleolus, but not prominently with PML nuclear bodies. |
Yeast two-hybrid screen, in vivo co-localization by GFP/RFP fusion proteins in HeLa cells, domain mapping of binding sites |
Cell biochemistry and biophysics |
Medium |
16679534
|
| 2015 |
SERBP1 is a component of the LRH1 (liver receptor homologue-1) transcriptional complex; LRH1 binds the SERBP1 promoter and represses SERBP1 transcription, while LRH1 knockdown increases SERBP1 expression. |
Nuclear fractionation followed by mass spectrometry and Western blot to identify LRH1-interacting partners, LRH1 siRNA knockdown, promoter:reporter luciferase assay |
Journal of proteome research |
Medium |
26398198
|
| 2013 |
SPINDLIN1 (SPIN1) interacts with SERBP1 via its Tudor-like domain to form a ribonucleoprotein complex that regulates mRNA stability and/or translation; this complex controls PDE3A mRNA levels and is required for meiotic resumption in mouse oocytes. |
Co-immunoprecipitation of SPIN1 with SERBP1, Spin1 conditional knockout in mouse oocytes with meiotic phenotype, PDE3A mRNA quantification |
PloS one |
Medium |
23894536
|
| 2024 |
SYT1 binds and stabilizes SERBP1 protein, which in turn enhances GLUT2 mRNA stability; this SYT1-SERBP1-GLUT2 axis promotes PQ efflux and protects kidney cells from paraquat toxicity. |
Immunoprecipitation-shotgun proteomics identifying SYT1-SERBP1 interaction, RNA interference of SERBP1, Western blot and mRNA stability assay for GLUT2 |
Chemico-biological interactions |
Medium |
39059605
|
| 2005 |
SERBP1 (PAIRBP1) localizes to the extracellular surface of granulosa and luteal cells and mediates progesterone's antiapoptotic action; immunoprecipitation with SERBP1 antibody co-pulls down PGRMC1, suggesting SERBP1 functions in a complex with this membrane progesterone-binding protein. |
Immunocytochemistry on non-permeabilized living cells, SERBP1 antibody blocking of P4 antiapoptotic action, immunoprecipitation pulling down PGRMC1 |
Biology of reproduction |
Medium |
15814896
|
| 2026 |
SERBP1 binds parallel G-quadruplex (G4) RNA and DNA structures with low micromolar affinity via its RGG box in an encircling mechanism; phosphomimetic mutations of C-terminal serine residues reduce G4 binding affinity, identifying phosphorylation as a regulatory switch. SERBP1 regulates mTOR expression in glioblastoma through G4 elements in the mTOR 5' UTR, and SERBP1 depletion synergizes with mTOR inhibition to reduce cell growth. |
NMR spectroscopy, biophysical binding assays, molecular dynamics and docking simulations, phosphomimetic mutagenesis, SERBP1 depletion in GBM cells with mTOR expression and growth readouts |
bioRxivpreprint |
Medium |
41846982
|
| 2025 |
In situ cryo-EM of human cells reveals that SERBP1 binds to the ribosome in almost all translating and non-translating states, bridging the 60S and 40S ribosomal subunits at multiple binding sites not observed on purified ribosomes. |
In situ cryo-EM of intact human cells using cryo-FIB milling and single-particle analysis (2.19 Å consensus structure with 21 functional states) |
bioRxivpreprint |
Medium |
bio_10.1101_2024.07.02.601723
|
| 2025 |
Cryo-EM at 1.72 Å of human 60S ribosome identifies SERBP1 bound at the peptidyl transferase center in a dormant, non-translating ribosome state, consistent with SERBP1 occupying the mRNA channel of non-translating ribosomes. |
High-resolution cryo-EM of human ribosomes in cell-free translation lysate |
bioRxivpreprint |
Medium |
bio_10.1101_2025.10.11.680285
|
| 2025 |
SERBP1 is required for oocyte growth and meiotic competence in mice; conditional Serbp1 knockout causes arrested oocyte growth, spindle assembly defects, impaired asymmetric division, granulosa cell apoptosis, and elevated ERK1/2 phosphorylation, leading to female infertility. |
Conditional knockout using Zp3/Gdf9-Cre drivers, spindle assembly immunofluorescence, ERK1/2 phosphorylation Western blot, phenotypic analysis of oocyte development and fertility |
Molecular and cellular endocrinology |
High |
40902969
|