ArticleMolecular and cellular biology2000
p300 requires its histone acetyltransferase activity and SRC-1 interaction domain to facilitate thyroid hormone receptor activation in chromatin.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 125 citations in OpenAlex.
- Transcriptional Cofactors for Thyroid Hormone Receptors.Endocrinology · 2025Review
- Steroid-receptor coactivator complexes in thyroid hormone-regulation of Xenopus metamorphosis.Vitamins and hormones · 2023Article
- Thyroid Hormone-mediated Histone Modification Protects Cortical Neurons From the Toxic Effects of Hypoxic Injury.Journal of the Endocrine Society · 2022Article
- A coregulator shift, rather than the canonical switch, underlies thyroid hormone action in the liver.Genes & development · 2021Article
- Switches in histone modifications epigenetically control vitamin D3-dependent transcriptional upregulation of the CYP24A1 gene in osteoblastic cells.Journal of cellular physiology · 2020Article
- Multiple mechanisms regulate H3 acetylation of enhancers in response to thyroid hormone.PLoS genetics · 2020Article
- Functional Studies of Transcriptional Cofactors via Microinjection-Mediated Gene Editing in Xenopus.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Mechanisms of Host IFI16, PML, and Daxx Protein Restriction of Herpes Simplex Virus 1 Replication.Journal of virology · 2018Article
- Histone methyltransferase Dot1L is a coactivator for thyroid hormone receptor duringFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017Article
- Agonist-mediated assembly of the crustacean methyl farnesoate receptor.Scientific reports · 2017Article
- Thyroid hormone regulation of adult intestinal stem cells: Implications on intestinal development and homeostasis.Reviews in endocrine & metabolic disorders · 2016Review
- Regulation of growth rate and developmental timing by Xenopus thyroid hormone receptor α.Development, growth & differentiation · 2016Review
- Selection and Application of DNA Aptamer Against Oncogene Amplified in Breast Cancer 1.Journal of molecular evolution · 2015Article
- Structure of a biologically active estrogen receptor-coactivator complex on DNA.Molecular cell · 2015Article
- Activation of the RhoB signaling pathway by thyroid hormone receptor β in thyroid cancer cells.PloS one · 2014Article
- Epigenetic regulation of thyroid hormone-induced adult intestinal stem cell development during anuran metamorphosis.Cell & bioscience · 2014Review
- Unliganded thyroid hormone receptor regulates metamorphic timing via the recruitment of histone deacetylase complexes.Current topics in developmental biology · 2013Review
- Thyroid hormone receptor actions on transcription in amphibia: The roles of histone modification and chromatin disruption.Cell & bioscience · 2012Article
- The role of AIB1 in breast cancer.Oncology letters · 2012Article
- The function of steroid receptor coactivator-1 in normal tissues and cancer.International journal of biological sciences · 2012Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We have characterized the mechanism by which coactivator p300 facilitates transcriptional activation mediated by the heterodimer of thyroid hormone (T3) receptor and 9-cis retinoid acid receptor (TR-RXR) in the context of chromatin. We demonstrate that, while p300 can enhance the transcriptional activation mediated by both liganded TR-RXR and GAL4-VP16, its histone acetyltransferase activity (HAT) is required for its ability to facilitate liganded TR-RXR- but not GAL4-VP16-mediated transcriptional activation. To understand how p300 is recruited by liganded TR-RXR, we have analyzed the interactions between TR-RXR and p300 as well as SRC-1 family coactivators. We show that, in contrast to a strong hormone-dependent interaction between TR-RXR and SRC-1 family coactivators, p300 displays minimal, if any, T3-dependent interaction with TR-RXR. However, p300 can be recruited by liganded TR-RXR through its interaction with SRC-1 family coactivators. Consistent with the protein-protein interaction profile described above, we demonstrate that the SRC-1 interaction domain of p300 is important for its ability to facilitate transcriptional activation mediated by TR-RXR, whereas its nuclear receptor interaction domain is dispensable. Collectively, these results reveal the functional significance of the HAT activity of p300 and define an indirect mode for the action of p300 in TR-RXR activation.
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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.