ArticleThe Biochemical journal2007
Deacetylation of the retinoblastoma tumour suppressor protein by SIRT1.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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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
79 citing papers in PubMed, 142 citations in OpenAlex.
- Arbutin as a promising cardioprotective anticancer adjuvant with doxorubicin in solid Ehrlich carcinoma through targeting NEK7-dependent inflammasome/SIRT1/caspase-3/oxidative stress pathways.Molecular and cellular biochemistry · 2026Article
- Post-translational modifications in retinoblastoma: mechanisms, immune regulation, and therapeutic opportunities.Frontiers in immunology · 2026Review
- Review
- Histone Deacetylases in Retinoblastoma.International journal of molecular sciences · 2024Review
- Conserved role of hnRNPL in alternative splicing of epigenetic modifiers enables B cell activation.EMBO reports · 2024Article
- Fluorescent nanodiamonds as innovative delivery systems for MiR-34a replacement in breast cancer.Molecular therapy. Nucleic acids · 2023Article
- Targeting the acetylation signaling pathway in cancer therapy.Seminars in cancer biology · 2022Review
- Nucleolar protein NOC4L inhibits tumorigenesis and progression by attenuating SIRT1-mediated p53 deacetylation.Oncogene · 2022Article
- Post-translational modifications on the retinoblastoma protein.Journal of biomedical science · 2022Review
- Role of sirtuins in esophageal cancer: Current status and future prospects.World journal of gastrointestinal oncology · 2022Review
- Regulation of SIRT1 and Its Roles in Inflammation.Frontiers in immunology · 2022Review
- Nicotinamide adenine dinucleotide and the sirtuins caution: Pro-cancer functions.Aging medicine (Milton (N.S.W)) · 2021Review
- Sirt1 deficiency upregulates glutathione metabolism to prevent hepatocellular carcinoma initiation in mice.Oncogene · 2021Article
- Trending topics of SIRT1 in tumorigenicity.Biochimica et biophysica acta. General subjects · 2021Review
- MicroRNA-217 inhibits the proliferation and invasion, and promotes apoptosis of non-small cell lung cancer cells by targeting sirtuin 1.Oncology letters · 2021Article
- Review
- Review
- Proliferation Increasing Genetic Engineering in Human Corneal Endothelial Cells: A Literature Review.Frontiers in medicine · 2021Review
- Biological Efficacy and Safety of Niacinamide in Patients With ADPKD.Kidney international reports · 2020Article
- Ubiquitination-mediated degradation of SIRT1 by SMURF2 suppresses CRC cell proliferation and tumorigenesis.Oncogene · 2020Article
19 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The activity of Rb (retinoblastoma protein) is regulated by phosphorylation and acetylation events. Active Rb is hypophosphorylated and acetylated on multiple residues. Inactivation of Rb involves concerted hyper-phosphorylation by cyclin-CDK (cyclin-dependent kinase) complexes combined with deacetylation of appropriate lysine residues within Rb. In the present study, using in vivo co-immunoprecipitation experiments, we identified mammalian SIRT1 (sirtuin 1) as a binding partner for Rb and its family members p107 and p130. Formation of Rb-SIRT1 complexes required the pocket domain of Rb. p300 catalysed the acetylation of Rb, and SIRT1 was a potent deacetylase for Rb. The ability of SIRT1 to catalyse the deacetylation of Rb was dependent on NAD and was inhibited by the SIRT1 inhibitor nicotinamide. Deacetylated lysine residues within Rb formed a domain similar to the SIRT1-targeted domain of the p53 tumour suppressor protein. Cultures of arrested cells, via contact inhibition or DNA damage, exhibited decreased Rb phosphorylation and increased Rb acetylation. Overexpression of SIRT1 in either confluent or etoposide-treated cells resulted in a significant reduction in Rb acetylation, which was restored with nicotinamide. Gene knockdown of SIRT1 by siRNA (short interfering RNA) produced an accumulation of acetylated Rb. This increase was augmented further when siRNA against SIRT1 was used in conjunction with nicotinamide. In conclusion, our results demonstrate that SIRT1 is an in vitro and in vivo deacetylase for the Rb tumour suppressor protein.
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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.