| 2006 |
RPS27L is a direct transcriptional target of p53: a consensus p53-binding site in the first intron of RPS27L drives p53-dependent transactivation, demonstrated by direct p53 binding in vitro and in vivo (ChIP), luciferase reporter assays, and sensitivity to dominant-negative p53 mutants. Overexpression of RPS27L promotes, and siRNA silencing inhibits, etoposide-induced apoptosis. |
ChIP, in vitro binding, luciferase reporter, siRNA knockdown, overexpression with apoptosis assay |
Oncogene |
High |
17057733
|
| 2007 |
RPS27L is a nuclear protein that forms nuclear foci upon DNA damage. Depletion of RPS27L causes deficiency in DNA damage checkpoints, converting p53-mediated cell cycle arrest to apoptosis, and RPS27L positively regulates p21 protein expression. |
siRNA knockdown, immunofluorescence/nuclear foci analysis, cell cycle and apoptosis assays, western blot for p21 |
Cancer research |
Medium |
18056458
|
| 2010 |
The N-terminal region of RPS27L binds to the central acidic domain of MDM2, forming an in vivo triplex complex with MDM2 and p53. RPS27L competes with p53 for MDM2 binding, inhibits MDM2-mediated p53 ubiquitination, and extends p53 protein half-life. RPS27L is itself a short-lived MDM2 substrate whose degradation requires the RING or acidic domain of MDM2. Upon p53-activating signals, RPS27L shuttles from cytoplasm to nucleoplasm where it colocalizes with MDM2. |
Co-immunoprecipitation, domain-mapping experiments, ubiquitination assay, protein half-life (CHX chase), siRNA knockdown, immunofluorescence/subcellular fractionation |
Oncogene |
High |
21170087
|
| 2014 |
In vivo mouse knockout shows that Rps27l disruption triggers ribosomal stress that stabilizes Mdm2, which then degrades Mdm4, reducing the Mdm2-Mdm4 E3 ligase activity toward p53 and leading to p53-dependent apoptotic depletion of hematopoietic stem cells and postnatal death rescued by Trp53 deletion. Under Trp53+/- background, Rps27l loss drives genomic instability and Trp53 LOH to promote lymphomagenesis. |
Germline knockout mice, genetic rescue (Trp53 deletion), western blot for Mdm2/Mdm4/p53 levels, hematopoietic stem cell assays, tumor incidence analysis, genome aneuploidy measurement |
eLife |
High |
25144937
|
| 2018 |
RPS27L silencing inactivates mTORC1 (but not mTORC2) and induces autophagy via the β-TrCP–DEPTOR axis: loss of RPS27L shortens β-TrCP protein half-life, causing DEPTOR accumulation that inhibits mTORC1. Simultaneous DEPTOR silencing partially rescues autophagy induction, establishing DEPTOR as a causal mediator. Autophagy inhibition with chloroquine or Bafilomycin A1 then triggers apoptosis in RPS27L-silenced cells. |
siRNA knockdown, protein half-life assay (CHX chase), mTOR pathway western blot, autophagy assays (LC3 flux), rescue experiments (DEPTOR co-knockdown), pharmacological inhibition |
Cell death & disease |
High |
30425236
|
| 2018 |
Rps27l inactivation causes radiosensitivity via two axes: (1) activated p53 pathway due to imbalanced Mdm2/Mdm4 levels and reduced E3 ligase activity; and (2) elevated Mdm2 binding to Nbs1 that inhibits Nbs1-Atm binding and subsequent Atm activation, reducing MRN/ATM-mediated DNA damage response. Heterozygous Mdm2 deletion restores the MRN/ATM signal. |
Rps27l−/−;Trp53+/− mice irradiation, western blot for Mdm2/Mdm4/p53/MRN/ATM, Co-IP of Mdm2-Nbs1, genetic rescue (Mdm2 heterozygous deletion), proliferation/apoptosis assays |
Cell death & disease |
High |
29396424
|
| 2020 |
Both RPS27L and RPS27 are subjected to neddylation by MDM2 E3 ligase and deneddylation by NEDP1. Blockage of neddylation with MLN4924 destabilizes RPS27L and RPS27 by shortening their protein half-lives. Knockdown of RPS27L/RPS27 sensitizes, and ectopic expression desensitizes, cancer cells to MLN4924-induced apoptosis, indicating that neddylation stabilizes these proteins for cancer cell survival. |
Neddylation assay, CHX chase (protein half-life), MLN4924 pharmacological inhibition, siRNA knockdown, overexpression, apoptosis assays |
FASEB journal |
Medium |
32779270
|
| 2020 |
RPS27L binds directly to FANCD2 and FANCI. Upon RPS27L knockdown, FANCD2 and FANCI levels decrease due to accelerated degradation via p62-mediated autophagy-lysosome pathway (abrogated by chloroquine or Beclin1 knockdown). RPS27L knockdown suppresses FANCD2 foci formation and impairs ICL repair after mitomycin C treatment. |
Co-immunoprecipitation, siRNA knockdown, western blot, chloroquine/Beclin1 rescue, FANCD2 immunofluorescence foci, MMC sensitivity assay |
Cell death & disease |
High |
33051438
|
| 2023 |
Rps27 and Rps27l are functionally equivalent proteins arising from vertebrate whole-genome duplication: expressing Rps27 protein from the endogenous Rps27l locus or vice versa completely rescues loss-of-function lethality. Despite equivalent protein function, the paralogs associate preferentially with different mRNA transcripts in ribosomes and show inversely correlated, cell-type-specific expression patterns, indicating subfunctionalized expression rather than divergent protein function. |
Endogenous protein tagging, knock-in rescue (protein swap), ribosome-mRNA association profiling, homozygous lethal loss-of-function allele comparison, RNA-seq expression analysis across cell types |
eLife |
High |
37306301
|
| 2025 |
PPP2R2C physically interacts with RPS27L (confirmed by IP-MS, Co-IP, and immunofluorescence) and stabilizes RPS27L protein by blocking proteasomal degradation (demonstrated by cycloheximide chase and proteasome inhibitor assays). RPS27L knockdown reverses PPP2R2C-mediated radioresistance and suppression of ferroptosis in nasopharyngeal carcinoma cells. |
IP-MS, Co-IP, immunofluorescence, cycloheximide chase, proteasome inhibition, siRNA knockdown, ferroptosis assays (lipid ROS, MDA, GPX4/SLC7A11 western blot, TEM) |
Cell death & disease |
Medium |
42115626
|
| 2025 |
RPS27L functions as an RNA-binding protein whose N-terminal intrinsically disordered region mediates liquid-liquid phase separation (LLPS). RPS27L interacts with IGF1 to regulate myogenesis. Muscle-specific Rps27l knock-in mice show increased muscle mass, enlarged myofibers, higher fast-twitch fiber proportion, and enhanced muscle regeneration. RPS27L expression is negatively regulated by the myogenic transcription factor SIX4. |
Muscle-specific knock-in mice, myofiber size/composition analysis, LLPS assay, Co-IP/interaction studies with IGF1, siRNA/overexpression in myoblasts, SIX4 transcription factor assays |
Advanced science |
Medium |
40886325
|
| 2025 |
Ribosome-associated factor Nufip1, highly expressed in long-lived bat fibroblasts, associates with ribosomal protein Rps27l and is proposed as an integrator of ribosomal and p53 signaling under DNA replication stress conditions. |
Comparative transcriptome analysis, co-association/interaction experiment (abstract does not specify Co-IP vs pulldown) |
Zoological research |
Low |
40407135
|