| 2024 |
The deubiquitinase OTUD6 deubiquitinates RPS7/eS7 specifically on the free 40S ribosome (not on 43S/48S initiation complexes or translating ribosomes), with the E3 ligases CNOT4 and RNF10 and the 40S protein RACK1 functioning upstream of OTUD6. OTUD6 protein abundance bidirectionally regulates global protein translation levels, suggesting OTUD6 promotes translation initiation by modulating the pool of free 40S ribosomes available for recycling. |
Coimmunoprecipitation, enrichment of monoubiquitinated proteins from catalytically inactive OTUD6 Drosophila, genetic epistasis in vivo, global protein translation assays |
Nature communications |
High |
39127721
|
| 2024 |
RPS7 functions as an RNA-binding protein that stabilizes LOXL2 mRNA by binding to AUUUA motifs in the 3155–3375 region of the LOXL2 3'-UTR, increasing LOXL2 mRNA abundance and protein expression, which in turn maintains ITGB1 protein stability and activates ITGB1-mediated FAK/SRC signaling to promote HCC cell adhesion, migration, invasion, and lung metastasis. |
RNA immunoprecipitation (RIP), RNA pull-down, RNA sequencing, dual luciferase reporter assay, nascent RNA capture assay, RNA decay assay, CRISPR-Cas9 knockout, gain- and loss-of-function analyses |
Journal of experimental & clinical cancer research : CR |
High |
38326908
|
| 2015 |
The viral oncoprotein HBx stabilizes SIRT7 deacetylase by preventing its ubiquitin-mediated proteasomal degradation; HBx-accumulated SIRT7 is recruited to the RPS7 promoter, promotes H3K18 deacetylation at that locus, and thereby represses RPS7 transcription. Inhibition of cellular deubiquitinase activity restored RPS7 transcription. |
Chromatin immunoprecipitation, ectopic expression of HBx, SIRT7 depletion, HBx transgenic mice, deubiquitinase inhibition assay, clonogenicity assay |
Scientific reports |
Medium |
26442981
|
| 2016 |
RPS7 inhibits colorectal cancer glycolysis by suppressing HIF-1α expression and downstream glycolytic proteins GLUT4 and LDHB; ectopic HIF-1α overexpression abrogates the growth-inhibitory effects of RPS7 overexpression, placing RPS7 upstream of HIF-1α in this pathway. |
RPS7 overexpression and knockdown in CRC cells, HIF-1α rescue experiments, in vivo xenograft assays, tissue microarray, Western blotting |
Oncotarget |
Medium |
26735579
|
| 2021 |
The protein methyltransferase SMYD2 activates RPS7 transcription by binding to the RPS7 promoter; SMYD2-driven increases in proliferation, migration, and invasion of lung adenocarcinoma cells are partially reversed by RPS7 knockdown, placing RPS7 downstream of SMYD2 in this oncogenic pathway. |
Chromatin immunoprecipitation-quantitative PCR, RNA-seq, SMYD2 knockdown and AZ505 inhibitor treatment, RPS7 rescue experiments, in vivo tumor growth assays |
Cell death & disease |
Medium |
33935284
|
| 2019 |
Kinase PIM1 is a component of the small 40S ribosomal subunit and regulates RPS7 protein levels; PIM1 enhances c-Myc protein stability, and c-Myc drives RPS7 transcription via a functional E-box motif upstream of the RPS7 transcription start site. RPS7 knockdown reduces prostate cancer cell growth in vitro and in vivo, and RPS7 overexpression rescues the condensed cellular body and decreased protein translation caused by PIM1 inhibition. |
Ribosomal subunit fractionation (PIM1 in 40S), E-box reporter assay, RPS7 knockdown and overexpression in PC3 cells, in vivo xenograft, Western blotting |
Carcinogenesis |
Medium |
30247545
|
| 2019 |
RPS7 knockdown in prostate cancer cells upregulates the epithelial marker E-cadherin and downregulates mesenchymal markers N-cadherin and Snail, indicating that RPS7 promotes cell migration by activating the epithelial-to-mesenchymal transition (EMT) pathway. |
RPS7 siRNA knockdown, Western blotting for EMT markers, transwell migration assay, MTT proliferation assay |
Urologic oncology |
Low |
30737160
|
| 2014 |
RPS7 physically interacts with 14-3-3γ and eIF1AX in bovine mammary epithelial cells, as established by co-immunoprecipitation/mass spectrometry, colocalization, and FRET analysis; overexpression of RPS7 promotes protein translation and cell proliferation. |
Co-immunoprecipitation, MALDI-TOF/TOF peptide mass fingerprinting, colocalization microscopy, FRET, overexpression studies |
Archives of biochemistry and biophysics |
Medium |
25281768
|
| 2009 |
The N-terminal region of eukaryotic rpS5 (the yeast/human ortholog of bacterial rpS7, corresponding to RPS7 family) is required for efficient translation initiation; N-terminal truncations of yeast rpS5 impair 40S subunit function and reduce recruitment of initiation factors eIF3 and eIF2 to the ribosome. |
Yeast complementation with truncated rpS5 variants, biochemical analysis of 40S subunit function, measurement of initiation factor recruitment |
Nucleic acids research |
Medium |
19969550
|
| 2026 |
The covalent molecular glue DPB recruits RPS7 to the E3 ubiquitin ligase MKRN2 (via covalent modification of MKRN2 Cys335), creating a neo-interface that leads to ubiquitination and proteasomal degradation of RPS7, triggering nucleolar stress and apoptosis selectively in p53-deficient NSCLC cells. |
Quantitative thiol-reactivity proteomics (QTRP), co-immunoprecipitation-mass spectrometry, site-directed mutagenesis, genetic knockout/rescue, biophysical assays, in vivo orthotopic mouse model |
British journal of pharmacology |
High |
41991154
|
| 2013 |
Rps7 loss-of-function in mouse results in decreased body size, skeletal abnormalities, white spotting, eye malformations, and CNS developmental defects; these phenotypes (excluding CNS defects) are ameliorated by Trp53 deficiency, placing Rps7 upstream of p53 in the shared ribosomal stress pathway. |
Mouse genetic models (Rps7(Mtu) and Rps7(Zma) mutations), Trp53 double-mutant epistasis, morphological and neuroanatomical phenotyping |
PLoS genetics |
Medium |
23382688
|
| 2022 |
A heterozygous missense mutation RPS7 p.V134F causes ribosomal stress activation and impairs protein translational activity in a cellular model, establishing a mechanistic link between this specific RPS7 variant and translational deficiency in Diamond-Blackfan anemia. |
Cellular model of RPS7 p.V134F variant, protein translational activity assays, ribosomal stress activation assays, erythrocyte metabolism analysis |
Blood cells, molecules & diseases |
Medium |
35871033
|
| 2024 |
Archaeal NusA2 is the evolutionary ancestor of eukaryotic ribosomal protein eS7 (RPS7); crystal structures of NusA2 reveal an N-terminal zinc finger followed by two KH-like domains that bind single-stranded RNA, and mutations in the zinc finger compromise structural integrity, supporting the structural homology between NusA2 and eS7. |
X-ray crystallography (3.1 Å and 1.68 Å), RNA-binding assays, mutagenesis, molecular dynamics simulations, structure-guided phylogenetic analysis |
Structure (London, England : 1993) |
Medium |
39504966
|
| 2025 |
In S. cerevisiae, the two RPS7 paralogs (RPS7A and RPS7B) are differentially regulated: deletion of RPS7A upregulates RPS7B mRNA but not vice versa; 3'-UTR sequences critically control the stability of both paralog mRNAs; Fhl1p is required for RPS7B but not RPS7A transcription; and Rps7Ap abundance regulates the activity of both promoters, establishing a buffering system for Rps7p production. |
Yeast gene deletion, 3'-UTR mutagenesis, mRNA stability assays, promoter activity assays, Fhl1p deletion epistasis |
PloS one |
Medium |
40445952
|