ArticleBiochemical and biophysical research communications2021
ACAA2 is a ligand-dependent coactivator for thyroid hormone receptor β1.
Article in Biochemical and biophysical research communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 7 citations in OpenAlex.
- Myocardial lipin1 protects the heart against ischemic injury by preserving lipid homeostasis.JCI insight · 2025Article
- Sex alters thyroid hormone's effect on protein O-GlcNAcylation in the aged mouse heart.BMC molecular and cell biology · 2025Article
- Nicotinamide riboside kinase-2 regulates metabolic adaptation in the ischemic heart.Journal of molecular medicine (Berlin, Germany) · 2023Article
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Authors and funding
2 authors at 2 institutions in 1 country.
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Abstract
Thyroid hormones (THs) play a critical role in the metabolic phenotype of the heart; and most of the effects involve transcriptional regulation via thyroid hormone receptors (TRs). TRs ability to form combinatorial complexes with an array of partners accounts for TRs physiological flexibility in modulating gene expression. To identify proteins that associate with TRβ1 in the heart we performed a pull-down assay on cardiac tissue using GST-TRβ1 as bait and identified the bound proteins by LC MS/MS. ACAA2, a mitochondrial thiolase enzyme, was identified as a novel interacting protein. We confirmed ACAA2 localized to the nucleus and using a luciferase reporter assay showed ACAA2 acted as a TH-dependent coactivator for TRβ1. ACAA2 showed an ability to bind to TR recognition sequences but did not alter TRβ1 DNA binding ability. Thus, ACAA2 as a novel TRβ1 associating protein opens a new paradigm to understanding how TH/TRs may be manipulated by energetic pathway molecules.
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