ArticleMolecular and cellular biology2002
The SIN3/RPD3 deacetylase complex is essential for G(2) phase cell cycle progression and regulation of SMRTER corepressor levels.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 71 citations in OpenAlex.
- The histone modification regulator, SIN3, plays a role in the cellular response to changes in glycolytic flux.PloS one · 2025Article
- RebL1 is required for macronuclear structure stability and gametogenesis inMarine life science & technology · 2024Article
- Histone Acetylation Enhancing Host Melanization in Response to Parasitism by an Endoparasitoid Wasp.Insects · 2024Article
- Rescuing lung development through embryonic inhibition of histone acetylation.Science translational medicine · 2024Article
- Analysis of the chromatin landscape and RNA polymerase II binding at SIN3-regulated genes.Biology open · 2023Article
- NetREX-CF integrates incomplete transcription factor data with gene expression to reconstruct gene regulatory networks.Communications biology · 2022Article
- Isoforms of the transcriptional cofactor SIN3 differentially regulate genes necessary for energy metabolism and cell survival.Biochimica et biophysica acta. Molecular cell research · 2022Article
- Histone deacetylase 3 is required for development and metamorphosis in the red flour beetle, Tribolium castaneum.BMC genomics · 2020Article
- A complex interplay between SAM synthetase and the epigenetic regulator SIN3 controls metabolism and transcription.The Journal of biological chemistry · 2020Article
- Histone concentration regulates the cell cycle and transcription in early development.Development (Cambridge, England) · 2019Article
- Histone deacetylase 1 suppresses Krüppel homolog 1 gene expression and influences juvenile hormone action inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Systematic Analysis of SIN3 Histone Modifying Complex Components During Development.Scientific reports · 2018Article
- The Transcriptional Corepressor SIN3 Directly Regulates Genes Involved in Methionine Catabolism and Affects Histone Methylation, Linking Epigenetics and Metabolism.The Journal of biological chemistry · 2017Article
- Article
- Genome-wide studies reveal novel and distinct biological pathways regulated by SIN3 isoforms.BMC genomics · 2016Article
- The N-terminal Region of Chromodomain Helicase DNA-binding Protein 4 (CHD4) Is Essential for Activity and Contains a High Mobility Group (HMG) Box-like-domain That Can Bind Poly(ADP-ribose).The Journal of biological chemistry · 2016Article
- The histone demethylase dKDM5/LID interacts with the SIN3 histone deacetylase complex and shares functional similarities with SIN3.Epigenetics & chromatin · 2016Article
- Disruption of Methionine Metabolism in Drosophila melanogaster Impacts Histone Methylation and Results in Loss of Viability.G3 (Bethesda, Md.) · 2015Article
- Stress-mediated Sin3B activation leads to negative regulation of subset of p53 target genes.Bioscience reports · 2015Article
- A genome-wide association study for nutritional indices in Drosophila.G3 (Bethesda, Md.) · 2015Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The SIN3 corepressor and RPD3 histone deacetylase are components of the evolutionarily conserved SIN3/RPD3 transcriptional repression complex. Here we show that the SIN3/RPD3 complex and the corepressor SMRTER are required for Drosophila G(2) phase cell cycle progression. Loss of the SIN3, but not the p55, SAP18, or SAP30, component of the SIN3/RPD3 complex by RNA interference (RNAi) causes a cell cycle delay prior to initiation of mitosis. Loss of RPD3 reduces the growth rate of cells but does not cause a distinct cell cycle defect, suggesting that cells are delayed in multiple phases of the cell cycle, including G(2). Thus, the role of the SIN3/RPD3 complex in G(2) phase progression appears to be independent of p55, SAP18, and SAP30. SMRTER protein levels are reduced in SIN3 and RPD3 RNAi cells, and loss of SMRTER by RNAi is sufficient to cause a G(2) phase delay, demonstrating that regulation of SMRTER protein levels by the SIN3/RPD3 complex is a vital component of the transcriptional repression mechanism. Loss of SIN3 does not affect global acetylation of histones H3 and H4, suggesting that the G(2) phase delay is due not to global changes in genome integrity but rather to derepression of SIN3 target genes.
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