The vitamin D receptor (VDR) binds to the nuclear matrix via its hinge domain: a potential mechanism for the reduction in VDR mediated transcription in mitotic cells

Cui, Xiaoying, Pertile, Renata and Eyles, Darryl W. (2017) The vitamin D receptor (VDR) binds to the nuclear matrix via its hinge domain: a potential mechanism for the reduction in VDR mediated transcription in mitotic cells. Molecular and Cellular Endocrinology, . doi:10.1016/j.mce.2017.11.015


Author Cui, Xiaoying
Pertile, Renata
Eyles, Darryl W.
Title The vitamin D receptor (VDR) binds to the nuclear matrix via its hinge domain: a potential mechanism for the reduction in VDR mediated transcription in mitotic cells
Journal name Molecular and Cellular Endocrinology   Check publisher's open access policy
ISSN 0303-7207
1872-8057
Publication date 2017-11-26
Sub-type Article (original research)
DOI 10.1016/j.mce.2017.11.015
Open Access Status Not yet assessed
Total pages 8
Place of publication E Park, Shannon, Clare Ireland
Publisher Elsevier Ireland
Language eng
Subject 1303 Biochemistry
1312 Molecular Biology
1310 Endocrinology
Abstract Vitamin D is best known for its regulation of calcium homeostasis. Vitamin D exerts its genomic actions via the vitamin D receptor (VDR). As a member of the superfamily of nuclear receptors (NR), the VDR is primarily located within the nucleus of non-dividing cells. We show here that the VDR relocates from the nucleus into the cytoplasm across all stages of cell division in CHO cells. Furthermore, we show that the VDR is transcriptionally inert during cell division. In addition, 1α, 25 dihydroxyvitamin D (1,25(OH)D) promotes VDR binding to the nuclear matrix. Finally, we assessed the structural nature of VDR binding to the nuclear matrix. Mutation of the hinge domain reduced VDR's ability to bind to the nuclear matrix and to initiate transcription in response to 1,25(OH)D. Taken together, our data suggest that the association between the VDR and the nuclear matrix accounts for the apparent cytosolic distribution as the matrix disperses within the cytoplasm when cells divide. This may also explain the dramatic reduction in VDR mediated transcription during cell division. Our data also confirm that similar to other NRs, the hinge domain of the VDR is responsible for this association.
Keyword Genomic functions
Mitosis
Mutant
Nuclear matrix
Nuclear receptor
Vitamin D
Vitamin D receptor
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
Queensland Brain Institute Publications
 
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Created: Thu, 30 Nov 2017, 13:44:32 EST by Kirstie Asmussen on behalf of Queensland Brain Institute