ArticleFrontiers in physiology2016
The Effects of Disease Models of Nuclear Actin Polymerization on the Nucleus.
Article in Frontiers in physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Coronary cytoskeletal modulation of coronary blood flow in the presence and absence of type 2 diabetes: the role of cofilin.Frontiers in physiology · 2025Article
- Article
- Nuclear actin filaments - a historical perspective.Nucleus (Austin, Tex.) · 2024Review
- The prophase oocyte nucleus is a homeostatic G-actin buffer.Journal of cell science · 2022Article
- Cytoskeleton integrity influences XRCC1 and PCNA dynamics at DNA damage.Molecular biology of the cell · 2021Article
- Profilin2 regulates actin rod assembly in neuronal cells.Scientific reports · 2021Article
- New Insights into Cellular Functions of Nuclear Actin.Biology · 2021Review
- Cardiomyocyte nuclearity and ploidy: when is double trouble?Journal of muscle research and cell motility · 2020Article
- Impairment of nuclear F-actin formation and its relevance to cellular phenotypes in Hutchinson-Gilford progeria syndrome.Nucleus (Austin, Tex.) · 2020Article
- Emerging roles of cytoskeletal proteins in regulating gene expression and genome organization during differentiation.Nucleus (Austin, Tex.) · 2020Review
- Profilin: many facets of a small protein.Biophysical reviews · 2020Review
- Indirect visualization of endogenous nuclear actin by correlative light and electron microscopy (CLEM) using an actin-directed chromobody.Histochemistry and cell biology · 2019Article
- Multiple Pools of Nuclear Actin.Anatomical record (Hoboken, N.J. : 2007) · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Actin plays a crucial role in regulating multiple processes within the nucleus, including transcription and chromatin organization. However, the polymerization state of nuclear actin remains controversial, and there is no evidence for persistent actin filaments in a normal interphase nucleus. Further, several disease pathologies are characterized by polymerization of nuclear actin into stable filaments or rods. These include filaments that stain with phalloidin, resulting from point mutations in skeletal α-actin, detected in the human skeletal disease intranuclear rod myopathy, and cofilin/actin rods that form in response to cellular stressors like heatshock. To further elucidate the effects of these pathological actin structures, we examined the nucleus in both cell culture models as well as isolated human tissues. We find these actin structures alter the distribution of both RNA polymerase II and chromatin. Our data suggest that nuclear actin filaments result in disruption of nuclear organization, which may contribute to the disease pathology.
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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.