The role of heat shock protein 70 in vitamin D receptor function.
The role of heat shock protein 70 in vitamin D receptor function.
复制标题
热休克蛋白 70 在维生素 D 受体功能中的作用。
DOI：
10.1006/bbrc.2001.4711
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发表时间：
2001
影响因子：
3.1
通讯作者：
Kumar,R
中科院分区：
文献类型：
--
作者：
Lutz,W;Kohno,K;Kumar,R
我们先前证明了1α，25-二羟基维生素D3受体（VDR）在体外与组成型热休克蛋白hsc 70相互作用，并与DnaK相互作用（Biochem. Biophys.通信资源260，446-452，1999）。然而，VDR-热休克蛋白相互作用的生物学意义尚不清楚。为了研究这种相互作用在真核细胞中的作用，我们在酿酒酵母中异源表达VDR和RXRα以及维生素D应答报告系统，并研究了这些细胞中热休克蛋白70基因（SSA）缺失的后果。我们表明，异源表达的VDR与酵母胞浆hsp 70蛋白，Ssa 1 p。SSA 2、SSA 3和SSA 4基因的缺失和Ssa 1 p活性的降低，降低了VDR及其异源二聚体伴侣RXRα的细胞内浓度，并降低了维生素D依赖性基因的活性。Hsp 70样分子伴侣蛋白在控制细胞内VDR浓度方面发挥作用。
We previously demonstrated that the 1α,25-dihydroxyvitamin D3receptor (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.