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Competitive Cofactor Recruitment by Orphan Receptor Hepatocyte Nuclear Factor 4α1: Modulation by the F Domain

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Ruse, Michael D., Privalsky, Martin L., Sladek, Frances M.·2002·Molecular and Cellular Biology
DOI 10.1128/mcb.22.6.1626-1638.2002PMC PMC135595
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Abstract

For most ligand-dependent nuclear receptors, the status of endogenous ligand modulates the relative affinities for corepressor and coactivator complexes. It is less clear what parameters modulate the switch between corepressor and coactivator for the orphan receptors. Our previous work demonstrated that hepatocyte nuclear factor 4alpha1 (HNF4alpha1, NR2A1) interacts with the p160 coactivator GRIP1 and the cointegrators CBP and p300 in the absence of exogenously added ligand and that removal of the F domain enhances these interactions. Here, we utilized transient-transfection analysis to demonstrate repression of HNF4alpha1 activity by the corepressor silencing mediator of retinoid and thyroid receptors (SMRT) in several cell lines and on several HNF4alpha-responsive promoter elements. Glutathione S-transferase pulldown assays confirmed a direct interaction between HNF4alpha1 and receptor interaction domain 2 of SMRT. Loss of the F domain resulted in marked reduction of the ability of SMRT to interact with HNF4alpha1 in vitro and repress HNF4alpha1 activity in vivo, although the isolated F domain itself failed to interact with SMRT. Surprisingly, loss of both the A/B and F domains restored full repression by SMRT, suggesting involvement of both domains in the SMRT interaction. Finally, we show that when coexpressed along with HNF4alpha1 and GRIP1, CBP, or p300, SMRT can titer out HNF4alpha1-mediated transactivation in a dose-dependent manner and that this competition derives from mutually exclusive binding. Collectively, these results suggest that HNF4alpha can functionally interact with both a coactivator and a corepressor without altering the status of any putative ligand and that the presence of the F domain may play a role in discriminating between the different coregulators.

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  • HNF4A has been shown to interact with the histone acetyltransferase p300, although whether this is direct or through the MLL4 complex has not been confirmed.

    “Moreover, HNF4A has been shown to interact with the histone acetyltransferase, p30062,63, although whether this is direct or through the MLL4 complex has not been confirmed.”

    From HNF4A guides the MLL4 complex to establish and maintain H3K4me1 at gene regulatory elements (2024) · cites this paper as [63]

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Authors
Ruse, M. D., Privalsky, M. L., & Sladek, F. M.
Affiliations
  • Biochemistry and Molecular Biology Graduate Program
  • University of California, Davis (US)
  • University of California, Riverside (US)
Corresponding author
Sladek, Frances M.
ORCID
Venue
Molecular and Cellular Biology
Publisher
Informa UK Limited
Published
2002-03-01
Volume
22
Issue
6
Pages
1626-1638
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
DOI
10.1128/mcb.22.6.1626-1638.2002
PMC
PMC135595
OpenAlex
W2168466279
Cited by
93
References
5
Citations by year
2026: 1 · 2025: 2 · 2024: 1 · 2023: 8 · 2022: 1 · 2021: 4 · 2020: 2 · 2019: 2 · 2018: 1 · 2016: 2 · 2015: 4 · 2013: 3 · 2012: 3
FWCI
3.15
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Molecular and Cellular Biology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK53528, DK 53892, R01DK053528, R01DK053892, R56DK053892)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords
orphan nuclear receptor, SMRT, corepressors, transcriptional coactivator, GRIP1, CBP, P300
MeSH terms
Animals, Binding, Competitive, Cell Line, Chlorocebus aethiops, DNA-Binding Proteins, Humans, Kidney, Ligands, Nuclear Proteins, Phosphoproteins, Protein Binding, Recombinant Fusion Proteins, Repressor Proteins, Transcription Factors, Transfection, Trans-Activators, Sequence Deletion, Protein Structure, Tertiary, Genes, Reporter, Receptors, Cytoplasmic and Nuclear, Two-Hybrid System Techniques, E1A-Associated p300 Protein, CREB-Binding Protein, Mice, Hepatocyte Nuclear Factor 4, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, Nuclear Receptor Coactivator 2, Nuclear Receptor Co-Repressor 2

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