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. 2019 Apr 4;20(7):1684. doi: 10.3390/ijms20071684

Figure 1.

Figure 1

N-terminal domain of RORα1 is sufficient for regulating target genes. (A) Illustration of the structure of RORα1, RORα4, RORα1ΔAF2, RORα4ΔAF2, RORα1ΔNTD, and RORα4 + 1NTD. (B) Luciferase assay was conducted using FLAG-pcDNA, RORα1, RORα4, RORα1ΔAF2, RORα4ΔAF2, RORα1ΔNTD, and RORα4 + 1NTD on a 5× RORE luciferase reporter. Values are expressed as mean ± SD for three independent experiments and normalized by β-galactosidase expression (mean ± SD, n = 3). The p value was calculated by a t-test (* p < 0.05, ** p < 0.01) or one-way ANOVA (*** p < 0.001). (C) Subcellular localization of GFP-pcDNA, GFP-RORα1, GFP-RORα4, GFP-RORα1ΔAF2, GFP-RORα4ΔAF2, GFP-RORα1ΔNTD, and GFP-RORα4 + 1NTD constructs (green). Nuclei were visualized by DAPI staining (blue). Scale bar, 20 μm. (D) Interaction of each in vitro transcribed and translated RORα1, RORα1ΔAF2, RORα1NTD and RORα4 constructs with glutathione S-transferase (GST) or GST fusion of β-catenin was assessed by GST pulldown assay. (E) Coimmunoprecipitation of endogenous β-catenin with each FLAG-tagged RORα construct.