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Related Experiment Videos

Vitamin D receptor contains multiple dimerization interfaces that are functionally different

J Nishikawa1, M Kitaura, M Imagawa

  • 1Department of Environmental Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University, Japan.

Nucleic Acids Research
|February 25, 1995
PubMed
Summary
This summary is machine-generated.

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The vitamin D receptor (VDR) forms dimers to signal. Researchers identified distinct VDR regions crucial for homodimerization and heterodimerization with retinoid X receptor (RXR), revealing specific interface functions.

Area of Science:

  • Molecular Biology
  • Endocrinology
  • Structural Biology

Background:

  • The vitamin D receptor (VDR) is essential for mediating the effects of 1 alpha, 25-dihydroxyvitamin D3.
  • VDR functions by binding to DNA through homodimers or heterodimers with the retinoid X receptor (RXR).

Purpose of the Study:

  • To map the specific dimerization interfaces of the VDR involved in homo- and heterodimer formation.
  • To elucidate the distinct roles of VDR regions in protein-protein interactions.

Main Methods:

  • Deletion mutagenesis of the VDR to identify critical regions for dimerization.
  • Analysis of VDR homodimerization and heterodimerization with RXR in the absence of DNA.

Main Results:

  • Deletion of the first zinc finger region impaired VDR homodimerization but not heterodimerization with RXR.

Related Experiment Videos

  • A region immediately following the zinc finger was critical for heterodimerization with RXR, but not homodimerization.
  • The carboxy-terminal region was essential for heterodimer formation and showed ligand-dependent enhancement of both homo- and heterodimerization.

    • Conclusions:

    • The VDR possesses at least three distinguishable dimerization interfaces.
    • These interfaces are located in the first zinc finger, the region beyond it, and the carboxy-terminal domain.
    • These findings provide insights into the structural basis of VDR-mediated signaling.