ArticleMolecular and cellular biology2009
Novel functions of protein arginine methyltransferase 1 in thyroid hormone receptor-mediated transcription and in the regulation of metamorphic rate in Xenopus laevis.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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47 citing papers in PubMed, 57 citations in OpenAlex.
- The dual function model revisited by thyroid hormone receptor knockouts: Unliganded state controlling the initiation of adult organ development while liganded state ensuring larval tissue resorption during metamorphosis.Developmental biology · 2026Review
- Understanding thyroid hormone receptor function in controlling developmental timing and rate in Xenopus: A journey from biochemistry and molecular biology to genetics.General and comparative endocrinology · 2026Review
- Knockout of protein arginine methyltransferase 1 inhibited cell growth and promoted cell migration in human bronchial epithelial cells.Scientific reports · 2025Article
- Thyroid hormone receptor subtype-specific function in controlling organ-specific developmental timing and rate duringFrontiers in endocrinology · 2025Review
- Functions and Mechanism of Thyroid Hormone Receptor Action During Amphibian Development.Endocrinology · 2024Review
- Protein arginine methyltransferase 1 regulates mouse enteroendocrine cell development and homeostasis.Cell & bioscience · 2024Article
- Intestinal remodeling during Xenopus metamorphosis as a model for studying thyroid hormone signaling and adult organogenesis.Molecular and cellular endocrinology · 2024Article
- Protein arginine methyltransferase 1 is required for the maintenance of adult small intestinal and colonic epithelial cell homeostasis.International journal of biological sciences · 2024Article
- Steroid-receptor coactivator complexes in thyroid hormone-regulation of Xenopus metamorphosis.Vitamins and hormones · 2023Article
- Essential and subtype-dependent function of thyroid hormone receptors during Xenopus metamorphosis.Vitamins and hormones · 2023Review
- Review
- How Protein Methylation Regulates Steroid Receptor Function.Endocrine reviews · 2022Review
- Protein arginine methyltransferase 1 regulates cell proliferation and differentiation in adult mouse adult intestine.Cell & bioscience · 2021Article
- Life Without Thyroid Hormone Receptor.Endocrinology · 2021Review
- The development of adult intestinal stem cells: Insights from studies on thyroid hormone-dependent anuran metamorphosis.Vitamins and hormones · 2021Article
- Knocking out histone methyltransferase PRMT1 leads to stalled tadpole development and lethality in Xenopus tropicalis.Biochimica et biophysica acta. General subjects · 2020Article
- A unique role of thyroid hormone receptor β in regulating notochord resorption during Xenopus metamorphosis.General and comparative endocrinology · 2019Article
- Canonical Wnt is inhibited by targeting one-carbon metabolism through methotrexate or methionine deprivation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Involvement of epigenetic modifications in thyroid hormone-dependent formation of adult intestinal stem cells during amphibian metamorphosis.General and comparative endocrinology · 2019Article
- Functional Studies of Transcriptional Cofactors via Microinjection-Mediated Gene Editing in Xenopus.Methods in molecular biology (Clifton, N.J.) · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Protein arginine methyltransferase 1 (PRMT1) acts as a transcription coactivator for nuclear receptors through histone H4 R3 methylation. The in vivo function of PRMT1 is largely unknown. Here we investigated the role of PRMT1 in thyroid hormone (T3) receptor (TR)-mediated transcription in vivo during vertebrate development. By using intestinal remodeling during T3-dependent Xenopus laevis metamorphosis for in vivo molecular analysis, we first showed that PRMT1 expression was upregulated during metamorphosis when both TR and T3 were present. We then demonstrated a role for PRMT1 in TR-mediated transcription by showing that PRMT1 enhanced transcriptional activation by liganded TR in the frog oocyte transcription system and was recruited to the T3 response element (TRE) of the target promoter in the oocyte, as well as to endogenous TREs during frog metamorphosis. Surprisingly, we found that PRMT1 was only transiently recruited to the TREs in the target during metamorphosis and observed no PRMT1 recruitment to TREs at the climax of intestinal remodeling when both PRMT1 and T3 were at peak levels. Mechanistically, we showed that overexpression of PRMT1 enhanced TR binding to TREs both in the frog oocyte model system and during metamorphosis. More importantly, transgenic overexpression of PRMT1 enhanced gene activation in vivo and accelerated both natural and T3-induced metamorphosis. These results thus indicate that PRMT1 functions transiently as a coactivator in TR-mediated transcription by enhancing TR-TRE binding and further suggest that PRMT1 has tissue-specific roles in regulating the rate of metamorphosis.
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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.