ArticleMolecular and cellular biochemistry2010
Irradiation with heavy-ion particles changes the cellular distribution of human histone acetyltransferase HAT1.
Article in Molecular and cellular biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- Newly synthesized histones: passive or active players in the regulation of epigenetic inheritance?Nucleic acids research · 2026Review
- Arabidopsis histone acetyltransferase complex coordinates cytoplasmic histone acetylation and nuclear chromatin accessibility.Science advances · 2024Article
- Bevacizumab induces ferroptosis and enhances CD8Acta pharmacologica Sinica · 2024Article
- Understanding HAT1: A Comprehensive Review of Noncanonical Roles and Connection with Disease.Genes · 2023Review
- Recent insights intoEpigenetics · 2021Review
- Histone Deacetylases Inhibitors in Neurodegenerative Diseases, Neuroprotection and Neuronal Differentiation.Frontiers in pharmacology · 2020Review
- Potential of Radiation-Induced Cellular Stress for Reactivation of Latent HIV-1 and Killing of Infected Cells.AIDS research and human retroviruses · 2016Article
- Therapeutic doses of irradiation activate viral transcription and induce apoptosis in HIV-1 infected cells.Virology · 2015Article
- Human histone acetyltransferase 1 (Hat1) acetylates lysine 5 of histone H2A in vivo.Molecular and cellular biochemistry · 2014Article
- The tale of protein lysine acetylation in the cytoplasm.Journal of biomedicine & biotechnology · 2011Review
- Histone acetyltransferase 1: more than just an enzyme?Biochimica et biophysica actaReview
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hat1 was the first histone acetyltransferase identified; however, its biological function is still unclear. In this report, it is shown for the first time that human Hat1 has two isoforms. Isoform a has 418 amino acids (aa) and is localized exclusively in the nuclear matrix of normal human keratinocytes (NHKs). Isoform b has 334 aa and is located in the cytoplasm, the nucleoplasm, attached to the chromatin and to the nuclear matrix. Immunohistochemical analyses revealed that the bulk of Hat1 is confined to the nucleus, with much lesser amounts in the cytoplasm. Cells undergoing mitotic division have an elevated amount of Hat1 compared to those that are non-mitotic. Senescent cells, however, exhibit a higher concentration of Hat1 in the cytoplasm compare to proliferating cells and the amount of Hat1 in the nucleus decreases with the progression of senescence. NHKs exposed to hydrogen peroxide (H(2)O(2)) or to a beam of high mass and energy ion particles displayed bright nuclear staining for Hat1, a phenotype that was not observed in NHKs exposed to gamma-rays. We established that the enhanced nuclear staining for Hat1 in response to these treatments is regulated by the PI3K and the mitogen-activated protein kinase signaling pathways. Our observations clearly implicate Hat1 in the cellular response assuring the survival of the treated cells.
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