ArticleOncogene2008
Ribosomal phosphoprotein P0 interacts with GCIP and overexpression of P0 is associated with cellular proliferation in breast and liver carcinoma cells.
Article in Oncogene, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 52 citations in OpenAlex.
- Value of altered methylation patterns of genes RANBP3, LCP2 and GRAP2 in cfDNA in breast cancer diagnosis.Journal of medical biochemistry · 2024Article
- Article
- DNA damage-induced paraspeckle formation enhances DNA repair and tumor radioresistance by recruiting ribosomal protein P0.Cell death & disease · 2022Article
- Cyclin D1 Binding Protein 1 Responds to DNA Damage through the ATM-CHK2 Pathway.Journal of clinical medicine · 2022Article
- An Improved Vector System for Homogeneous and Stable Gene Regulation.International journal of molecular sciences · 2021Article
- Identification and Characterization of P0 Protein as a Vaccine Candidate AgainstFrontiers in veterinary science · 2021Article
- CCNDBP1, a Prognostic Marker Regulated by DNA Methylation, Inhibits Aggressive Behavior in Dedifferentiated LiposarcomaFrontiers in oncology · 2021Article
- Serum and tissue proteomic signatures of patients with hepatocellular carcinoma using 2‑D gel electrophoresis.Molecular medicine reports · 2019Article
- Article
- Immunogenic Evaluation of Ribosomal P-Protein Antigen P0, P1, and P2 and Pentameric Protein Complex P0-(P1-P2)Journal of immunology research · 2019Article
- A Novel Systems-Biology Algorithm for the Analysis of Coordinated Protein Responses Using Quantitative Proteomics.Molecular & cellular proteomics : MCP · 2016Article
- Article
- Natural humoral immune response to ribosomal P0 protein in colorectal cancer patients.Journal of translational medicine · 2015Article
- The OsSec18 complex interacts with P0(P1-P2)2 to regulate vacuolar morphology in rice endosperm cell.BMC plant biology · 2015Article
- Evidence for a Role of the Transcriptional Regulator Maid in Tumorigenesis and Aging.PloS one · 2015Article
- A SILAC-based proteomics elicits the molecular interactome of alisertib (MLN8237) in human erythroleukemia K562 cells.American journal of translational research · 2015Article
- Article
- GCIP functions as a tumor suppressor in non-small cell lung cancer by suppressing Id1-mediated tumor promotion.Oncotarget · 2014Article
- Proteomic analysis of differentially expressed proteins in peripheral cholangiocarcinoma.Cancer microenvironment : official journal of the International Cancer Microenvironment Society · 2010Article
- Inhibition of protein phosphorylation in MIA pancreatic cancer cells: confluence of metabolic and signaling pathways.Journal of proteome research · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ribosomal acidic P0 protein, an essential component of the eukaryotic ribosomal stalk, was found to interact with the helix-loop-helix protein human Grap2 and cyclin D interacting protein (GCIP)/D-type cyclin-interacting protein 1/human homolog of MAID protein. Using in vivo and in vitro binding assays, we show that P0 can interact with the N and C termini of GCIP via its N-terminal 39-114 amino-acid residues. Although the P0-GCIP complex was detected mainly in cytoplasmic fraction, polysome profile analysis indicated that the P0-GCIP complex did not coelute with either polysomes or 60S ribosomes, suggesting that GCIP associates with the free form of P0 in the cytoplasm. Transfection of GCIP into MCF-7 cells resulted in decreased levels of pRb phosphorylation. Cotransfection of P0 with GCIP, however, resulted in GCIP-mediated reduction of pRb phosphorylation level which was repressed by P0. Furthermore, overexpression of P0 in breast cancer and hepatocellular cancer cell lines promoted cell growth and colony formation compared to control transfectants. Overexpression of P0 also increased cyclin D1 expression and phosphorylation of pRb at Ser780. Interestingly, P0 mRNA was overexpressed in 12 of 20 pairs of breast cancer/ normal breast specimens (60%). Together, these data indicate that P0 overexpression may cause tumorigenesis in breast and liver tissues at least in part by inhibiting GCIP-mediated tumor suppression.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.