ArticleGenes & cancer2012
Posttranslational modifications of the retinoblastoma tumor suppressor protein as determinants of function.
Article in Genes & cancer, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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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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Who cites it
43 citing papers in PubMed, 71 citations in OpenAlex.
- Tumor heterogeneity in retinoblastoma: a literature review.Cancer metastasis reviews · 2025Review
- Patterns in the tapestry of chromatin-bound RB.Trends in cell biology · 2024Review
- Article
- Mathematically Modeling the Effect of Endocrine and Cdk4/6 Inhibitor Therapies on Breast Cancer Cells.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Proteogenomic analysis of lung adenocarcinoma reveals tumor heterogeneity, survival determinants, and therapeutically relevant pathways.Cell reports. Medicine · 2022Article
- Targeting the acetylation signaling pathway in cancer therapy.Seminars in cancer biology · 2022Review
- Post-translational modifications on the retinoblastoma protein.Journal of biomedical science · 2022Review
- In Silico and Cellular Differences Related to the Cell Division Process between the A and B Races of the Colonial MicroalgaBiomolecules · 2021Article
- Arsenic trioxide reduces the expression of E2F1, cyclin E, and phosphorylation of PI3K signaling molecules in acute leukemia cells.Environmental toxicology · 2021Article
- Immunoblot Validation of Phospho-Specific Antibodies Using Lung Cancer Cell Lines.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Inhibition of MUC1 exerts cell-cycle arrest and telomerase suppression in glioblastoma cells.Scientific reports · 2020Article
- Review
- Mathematical modelling of breast cancer cells in response to endocrine therapy and Cdk4/6 inhibition.Journal of the Royal Society, Interface · 2020Article
- Beyond What Your Retina Can See: Similarities of Retinoblastoma Function between Plants and Animals, from Developmental Processes to Epigenetic Regulation.International journal of molecular sciences · 2020Review
- Rho kinase-dependent apical constriction counteracts M-phase apical expansion to enable mouse neural tube closure.Journal of cell science · 2019Article
- G1/S cell cycle regulators mediate effects of circadian dysregulation on tumor growth and provide targets for timed anticancer treatment.PLoS biology · 2019Article
- Targeting retinoblastoma protein phosphorylation in combination with EGFR inhibition in pancreatic cancer cells.International journal of oncology · 2019Article
- The RASSF6 Tumor Suppressor Protein Regulates Apoptosis and Cell Cycle Progression via Retinoblastoma Protein.Molecular and cellular biology · 2018Article
- Detection of Retinoblastoma Protein Phosphorylation by Immunoblot Analysis.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The retinoblastoma tumor suppressor protein (pRB) plays an integral role in G1-S checkpoint control and consequently is a frequent target for inactivation in cancer. The RB protein can function as an adaptor, nucleating components such as E2Fs and chromatin regulating enzymes into the same complex. For this reason, pRB's regulation by posttranslational modifications is thought to be critical. pRB is phosphorylated by a number of different kinases such as cyclin dependent kinases (Cdks), p38 MAP kinase, Chk1/2, Abl, and Aurora b. Although phosphorylation of pRB by Cdks has been extensively studied, activities regulated through phosphorylation by other kinases are just starting to be understood. As well as being phosphorylated, pRB is acetylated, methylated, ubiquitylated, and SUMOylated. Acetylation, methylation, and SUMOylation play roles in pRB mediated gene silencing. Ubiquitinylation of pRB promotes its degradation and may be used to regulate apoptosis. Recent proteomic data have revealed that pRB is posttranslationally modified to a much greater extent than previously thought. This new information suggests that many unknown pathways affect pRB regulation. This review focuses on posttranslational modifications of pRB and how they influence its function. The final part of the review summarizes new phosphorylation sites from accumulated proteomic data and discusses the possibilities that might arise from this data.
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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.