ArticleProceedings of the National Academy of Sciences of the United States of America2003
An actin-ribonucleoprotein interaction is involved in transcription by RNA polymerase II.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed.
- Nuclear actin-dependent Meg3 expression suppresses metabolic genes by affecting the chromatin architecture at sites of elevated H3K27 acetylation levels.Nucleic acids research · 2025Article
- Nuclear actin filaments - a historical perspective.Nucleus (Austin, Tex.) · 2024Review
- Non-Canonical Localization of Cardiac Troponins: Expanding Functions or Causing Pathologies?International journal of molecular sciences · 2024Review
- PIP2-Effector Protein MPRIP Regulates RNA Polymerase II Condensation and Transcription.Biomolecules · 2023Article
- Transcriptomics analysis of ethanol treatment of maleFrontiers in physiology · 2023Article
- Wiskott-Aldrich syndrome protein forms nuclear condensates and regulates alternative splicing.Nature communications · 2022Article
- Nuclear Actin Dynamics in Gene Expression, DNA Repair, and Cancer.Results and problems in cell differentiation · 2022Article
- The Role of Nuclear Actin in Genome Organization and Gene Expression Regulation During Differentiation.Results and problems in cell differentiation · 2022Review
- Review
- New Insights into Cellular Functions of Nuclear Actin.Biology · 2021Review
- Journey to the Center of the Cell: Cytoplasmic and Nuclear Actin in Immune Cell Functions.Frontiers in cell and developmental biology · 2021Review
- Emerging roles of cytoskeletal proteins in regulating gene expression and genome organization during differentiation.Nucleus (Austin, Tex.) · 2020Review
- Mechanosensing dysregulation in the fibroblast: A hallmark of the aging heart.Ageing research reviews · 2020Review
- Cytoskeletal proteins in the cell nucleus: a special nuclear actin perspective.Molecular biology of the cell · 2019Review
- Nuclear actin interactome analysis links actin to KAT14 histone acetyl transferase and mRNA splicing.Journal of cell science · 2019Article
- AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells.Bioscience reports · 2019Article
- Nuclear Actin: From Discovery to Function.Anatomical record (Hoboken, N.J. : 2007) · 2018Review
- Nuclear actin: ancient clue to evolution in eukaryotes?Histochemistry and cell biology · 2018Review
- Nuclear speckles: molecular organization, biological function and role in disease.Nucleic acids research · 2017Review
- Nuclear Actin in Development and Transcriptional Reprogramming.Frontiers in genetics · 2017Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To determine the function of actin in the cell nucleus, we sought to identify nuclear actin-binding proteins in the dipteran Chironomus tentans using DNase I-affinity chromatography. We identified the RNA-binding protein hrp65 as an actin-binding protein and showed that the C-terminal sequence of the hrp65-2 isoform is able to interact directly with actin in vitro. In vivo crosslinking and coimmunoprecipitation experiments indicated that hrp65 and actin are also associated in the living cell. Moreover, in vivo administration of a competing peptide corresponding to the C-terminal sequence of hrp65-2 disrupted the actin-hrp65-2 interaction and caused a specific and drastic reduction of transcription as judged by puff regression and diminished bromo-UTP incorporation. Our results indicate that an actin-based mechanism is implicated in the transcription of most if not all RNA polymerase II genes and suggest that an actin-hrp65-2 interaction is required to maintain the normal transcriptional activity of the cell. Furthermore, immunoelectron microscopy experiments and nuclear run-on assays suggest that the actin-hrp65-2 complex plays a role in transcription elongation.
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