The role of heat shock protein 70 in vitamin D receptor function

Ward Lutz, Kenji Kohno, Rajiv Kumar

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


We previously demonstrated that the 1α,25-dihydroxyvitamin D3 receptor (VDR) interacts with the constitutive heat shock protein, hsc70 in vitro, and with DnaK (Biochem. Biophys. Res. Commun. 260, 446-452, 1999). The biological significance of VDR-heat shock protein interactions, however, is unknown. To examine the role of such interactions in eukaryotic cells, we heterologously expressed VDR and RXRα together with a vitamin D-responsive reporter system in Saccharomyces cerevisiae and examined the consequences of heat shock protein 70 gene (SSA) deletion in these cells. We show that heterologously expressed VDR associates with the yeast cytosolic hsp70 protein, Ssa1p. Deletion of the SSA2, SSA3, and SSA4 genes and reduction of Ssa1p activity, reduces the intracellular concentrations of the VDR and its heterodimeric partner, RXRα and reduces the activity of a vitamin D-dependent gene. Hsp70-like chaperone proteins play a role in controlling concentrations of the VDR within the cell.

Original languageEnglish (US)
Pages (from-to)1211-1219
Number of pages9
JournalBiochemical and Biophysical Research Communications
Issue number5
StatePublished - 2001


  • Chaperones
  • Heat shock protein 70
  • Vitamin D receptor

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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