| 2007 |
PRMT3 (a type I arginine methyltransferase) directly methylates ribosomal protein rpS2 (RPS2/uS5) at arginine residues; PRMT3 is tethered to ribosomes via its interaction with rpS2, which is also its substrate. In PRMT3-knockout mice, rpS2 is hypomethylated, establishing rpS2 as a bona fide in vivo PRMT3 substrate that cannot be compensated by other PRMTs. |
Targeted gene disruption (PRMT3 knockout mice), Western blot for methylarginine, ribosome fractionation (polysome profiling), co-fractionation assays |
The Journal of biological chemistry |
High |
17439947
|
| 2009 |
In budding yeast Saccharomyces cerevisiae, which lacks a zinc-finger-containing Rmt3/PRMT3 homolog, Rps2 is partially modified to asymmetric dimethylarginine and monomethylarginine by the major arginine methyltransferase Rmt1, demonstrating organism-specific methyltransferase usage for the same substrate. |
Arginine methylation assays, methyltransferase deletion strains, mass spectrometry/biochemical detection of methylarginine |
Biochemical and biophysical research communications |
Medium |
20035717
|
| 2008 |
In fission yeast, Rps2 is required for nuclear export competence of pre-40S ribosomal subunits; its depletion causes retention of pre-40S particles in the nucleolus, blocks 40S subunit production, and impairs cleavage at site A2 within 32S pre-rRNA. |
Genetic depletion of Rps2 in Schizosaccharomyces pombe, pre-rRNA processing analysis, rRNA pulse-chase assays, nucleolar retention assays |
Nucleic acids research |
High |
18820293
|
| 2018 |
Human zinc finger protein ZNF277 forms an extraribosomal complex with uS5 (RPS2) in the cytoplasm and nucleolus using a C2H2-type zinc finger domain. ZNF277 and PRMT3 compete for uS5 binding: PRMT3 overexpression inhibits ZNF277-uS5 complex formation, and ZNF277 depletion increases uS5-PRMT3 levels. ZNF277 recognizes nascent uS5 co-translationally. |
Quantitative proteomics (affinity purification-MS), Co-IP in human cells, proximity ligation assay, overexpression/depletion experiments, subcellular fractionation |
The Journal of biological chemistry |
High |
30530495
|
| 2019 |
Tsr4 is a dedicated cytoplasmic chaperone for Rps2 (uS5) in S. cerevisiae. Tsr4 associates with Rps2 co-translationally, requires the eukaryote-specific N-terminal extension of Rps2 for interaction, promotes Rps2 solubility and expression, and is restricted to the cytoplasm despite Rps2 assembling into nuclear pre-40S particles. |
Co-translational co-IP, genetic depletion/perturbation of Tsr4, ribosome biogenesis assays, subcellular fractionation, yeast genetics |
Molecular and cellular biology |
High |
31182640
|
| 2020 |
Human PDCD2 functions as a dedicated ribosomal protein chaperone for uS5 (RPS2); PDCD2-uS5 complex is assembled co-translationally. Loss of PDCD2 impairs accumulation of soluble uS5 and its incorporation into 40S ribosomal subunits, causing defects in small ribosomal subunit synthesis that phenocopy uS5 deficiency. |
Quantitative proteomics (affinity purification-MS), co-translational Co-IP, PDCD2 knockdown with ribosome biogenesis readouts, polysome profiling |
Nucleic acids research |
High |
33245768
|
| 2016 |
In Drosophila, Zfrp8/PDCD2 directly interacts with RpS2 (uS5) of the 40S small ribosomal subunit. Zfrp8/PDCD2 regulates cytoplasmic levels of 40S ribosomal subunit components and controls cytoplasmic localization of specific mRNAs; knockdown causes nuclear accumulation of specific mRNAs and TE transcripts, suggesting Zfrp8 functions at late stages of ribosome assembly. |
Co-IP (Zfrp8-RpS2 pulldown), fluorescent tagging of ribosomal proteins, genetic knockdown (RNAi), RNA localization assays |
PloS one |
Medium |
26807849
|
| 2022 |
Ribosomal protein uS5/Rps2 residues at the mRNA entry channel of the 40S subunit influence start codon recognition in vivo; nonlethal substitutions of conserved Rps2 residues reduce bulk translation initiation, increase discrimination against poor initiation codons (near-cognate UUG and suboptimal Kozak context AUG), resembling substitutions in uS3/Rps3 and initiation factors eIF1/eIF1A. |
Site-directed mutagenesis of Rps2 residues, yeast genetic assays for translation initiation fidelity (UUG initiation reporters, Kozak context reporters), epistasis with known initiation mutants |
Genetics |
High |
34791232
|
| 2017 |
Mutations in the loop 2 region (residues 20–31) of ribosomal protein uS5 in E. coli confer spectinomycin resistance and affect translational fidelity; a minority of loop 2 mutants also show altered rRNA processing or ribosome biogenesis defects, demonstrating that this region participates in subunit assembly and maintenance of translational accuracy. |
Site-directed mutagenesis (21 unique mutants), spectinomycin sensitivity assays, translational fidelity reporters, rRNA processing analysis |
Antimicrobial agents and chemotherapy |
High |
27855073
|
| 2024 |
In S. cerevisiae, the cyclin-dependent kinase pathway (via Ypk2) phosphorylates Ser176 of uS5 (RPS2), which is located at the uS4-uS5 interface; phospho-Ser176 forms a salt bridge with Arg57 of uS4, strengthening the interface and increasing decoding selectivity. A second kinase pathway involving TORC1 and Pkc1 opposes this phosphorylation, indicating that translational accuracy is dynamically regulated by competing phosphorylation on uS5. |
Site-directed mutagenesis of Ser176 and Arg57, genetic epistasis analysis with kinase mutants (ctk1, ypk2, TORC1, pkc1), translational fidelity reporters |
Nucleic acids research |
Medium |
38340338
|
| 2023 |
Nuclear import of Rps2 (uS5) in yeast requires two distinct import signals: (1) an internal region (amino acids 76–145) that interacts with the importin-β Pse1, with Arg95, Arg97, and Lys99 being critical determinants; (2) an N-terminal region (amino acids 10–28) containing basic residues that constitutes a second import pathway. Both pathways function independently of the dedicated chaperone Tsr4. |
GFP reporter nuclear import assays, deletion/mutation analysis of Rps2 import signals, Co-IP with Pse1, genetic dissection in yeast |
Biomolecules |
Medium |
37509163
|
| 2022 |
Heliangin (a sesquiterpene lactone) covalently binds to the C222 site of RPS2, disrupting pre-rRNA metabolic processes, causing nucleolar stress, and activating the ribosomal proteins–MDM2–p53 pathway with consequent p53 stabilization in NPM1-mutant AML cells. |
Quantitative thiol reactivity platform screening, molecular biology validation, covalent binding assays, pre-rRNA processing assays, Western blot for p53/MDM2 |
Acta pharmaceutica Sinica. B |
Medium |
36873185
|
| 2010 |
RPS2 specifically binds pre-let-7a-1 RNA and blocks its processing to mature let-7a/let-7f miRNA in prostate cancer cells; this was shown by EMSA, antibody supershift assay, and immunoprecipitation. Overexpression of RPS2 correlates with loss of let-7a and elevated ras/c-myc, while RPS2 knockdown restores let-7a and reduces oncogene expression and tumorigenesis. |
EMSA, antibody supershift assay, immunoprecipitation, stable transfection/shRNA knockdown, Northern blot, immunofluorescence, SCID mouse tumor model |
Molecular cancer research : MCR |
Medium |
21148031
|
| 2025 |
RACK1 stabilizes RPS2 by inhibiting ubiquitin-mediated proteasomal degradation of RPS2; RACK1 knockdown increases RPS2 ubiquitination and accelerates its degradation (reversed by MG132). Both RACK1 and RPS2 positively regulate the NF-κB pathway, and RPS2 overexpression partially rescues the NF-κB inhibition caused by RACK1 knockdown in glioma cells. |
Co-immunoprecipitation, ubiquitination assays, MG132 proteasome inhibitor treatment, Western blot, NF-κB luciferase reporter assay, siRNA knockdown |
Molecular biology reports |
Medium |
40522528
|
| 2026 |
A 30-amino-acid N-terminal region of uS5 (RPS2) is necessary and sufficient for interaction with its dedicated chaperone PDCD2; a conserved FxxGFG motif within this region mediates hydrophobic interactions with PDCD2. An 11-amino-acid uS5-derived peptide that inhibits PDCD2-uS5 interaction impairs cancer cell viability. |
Affinity purification assays, structural modeling, complementation-based biosensor in human cells and cell extracts, deletion/mutation analysis, cell viability assays |
The Journal of biological chemistry |
Medium |
41933732
|
| 2025 |
In the absence of eIF2A, ubiquitination of RPS2 (and RPS3) is specifically diminished upon ribosome stalling, and eIF2A antagonizes USP10-dependent rescue of 40S ribosomes; this places RPS2 ubiquitination in a ribosome-associated quality control pathway regulated by eIF2A. |
TurboID proximity labeling combined with mass spectrometry, polysome gradient fractionation, eIF2A knockout cells, dynamic SILAC mass spectrometry, 40S footprinting |
bioRxivpreprint |
Low |
|