Identification of a novel melatonin-binding nuclear receptor: Vitamin D receptor

Fang, Nan; Hu, Chunyi; Sun, Wenqi; Xu, Ying; Gu, Yeqi; Wu, Le; Peng, Qing; Reiter, Russel J.; Liu, Lifeng

doi:10.1111/jpi.12618

Cited by 46Circadian rhythm and melatoninVitamin D Research StudiesBone Metabolism and Diseases

Identification of a novel melatonin-binding nuclear receptor: Vitamin D receptor

Fang, Nan, Hu, Chunyi, Sun, Wenqi, Xu, Ying, Gu, Yeqi, Wu, Le, Peng, Qing, Reiter, Russel J. +1 more·2020·Journal of Pineal Research

DOI 10.1111/jpi.12618

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Abstract

Previous studies confirmed that melatonin regulates Runx2 expression but the mechanism is unclear. There is a direct interaction between Runx2 and the vitamin D receptor (VDR). Herein, we observed a direct interaction between melatonin and the VDR but not Runx2 using isothermal titration calorimetry. Furthermore, this direct binding was detected only in the C-terminal ligand binding domain (LBD) of the VDR but not in the N-terminal DNA-binding domain (DBD) or the hinge region. Spectrophotometry indicated that melatonin and vitamin D3 (VD3) had similar uptake rates, but melatonin's uptake was significantly inhibited by VD3 until the concentration of melatonin was obviously higher than that of VD3 in a preosteoblastic cell line MC3T3-E1. GST pull-down and yeast two-hybrid assay showed that the interactive smallest fragments were on the 319-379 position of Runx2 and the N-terminus 110-amino acid DBD of the VDR. Electrophoretic mobility shift assay (EMSA) demonstrated that Runx2 facilitated the affinity between the VDR and its specific DNA substrate, which was further documented by a fluorescent EMSA assay where Cy3 labeled Runx2 co-localized with the VDR-DNA complex. Another fluorescent EMSA assay confirmed that the binding of the VDR to Runx2 was significantly enhanced with an increasing concentrations of the VDR, especially in the presence of melatonin; it was further documented using a co-immunoprecipitation assay that this direct interaction was markedly enhanced by melatonin treatment in the MC3T3-E1 cells. Thus, the VDR is a novel melatonin-binding nuclear receptor, and melatonin indirectly regulates Runx2 when it directly binds to the LBD and the DBD of the VDR, respectively.

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Melatonin can bind the vitamin D receptor (VDR), resulting in an enhancement of vitamin D's signaling effects and subsequent cellular activities.
“Most relevant for the discussion of this paper is that it can bind the vitamin D receptor (VDR), resulting in an enhancement of vitamin D’s signaling effects and subsequent cellular activities [18].”
From Is Melatonin the “Next Vitamin D”?: A Review of Emerging Science, Clinical Uses, Safety, and Dietary Supplements (2022) · cites this paper as [18]

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“Most relevant for the discussion of this paper is that it can bind the vitamin D receptor (VDR), resulting in an enhancement of vitamin D’s signaling effects and subsequent cellular activities [18].”
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Authors: Fang, N., Hu, C., Sun, W., Xu, Y., Gu, Y., Wu, L., Peng, Q., Reiter, R. J., & Liu, L.
Affiliations: Tongji University (CN)
Chinese Academy of Sciences (CN)
The University of Texas at San Antonio Health Science Center (US)
Corresponding author: Liu, Lifeng
ORCID: Fang, Nan
Hu, Chunyi
Sun, Wenqi
Xu, Ying
Wu, Le
Reiter, Russel J.
Liu, Lifeng
Venue: Journal of Pineal Research
Publisher: Wiley
Published: 2019-11-11
Volume: 68
Issue: 1
Pages: e12618-e12618
ISSN: 0742-3098 (ISSN-L)
1600-079X
DOI: 10.1111/jpi.12618
OpenAlex: W2982254695
Cited by: 46
References: 67
Citations by year: 2026: 2 · 2025: 6 · 2024: 8 · 2023: 6 · 2022: 5 · 2021: 8 · 2020: 10 · 2019: 1
FWCI: 3.31
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Journal of Pineal Research (publishedVersion)
PubMed (publishedVersion)
Funders: National Natural Science Foundation of China (81770870)
Topics: Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Circadian rhythm and melatonin
Health Sciences › Medicine › Pathology and Forensic Medicine › Vitamin D Research Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
Keywords: melatonin, vitamin D receptor, Runx2, nuclear receptor binding, ligand-binding domain, DNA-binding domain, vitamin D3, protein-protein interaction, transcriptional regulation, osteoblasts, MC3T3-E1 cells
MeSH terms: Protein Domains, Animals, Cell Line, Humans, Melatonin, Protein Binding, Receptors, Calcitriol, Core Binding Factor Alpha 1 Subunit, Mice, HEK293 Cells

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Identification of a novel melatonin-binding nuclear receptor: Vitamin D receptor

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