维甲酸相关孤儿受体α（RORα）的类泛素化修饰增强转录激活功能。
SUMOylation of RORalpha potentiates transcriptional activation function.
作者信息
Hwang Eun Ju, Lee Ji Min, Jeong Jiyeong, Park Joo Hyeon, Yang Young, Lim Jong-Seok, Kim Jung Hwa, Baek Sung Hee, Kim Keun Il
机构信息
Department of Biological Sciences, Research Center for Women's Disease, Sookmyung Women's University, 52 Hyochangwon-gil, Yongsan-gu, Seoul 140-742, South Korea.
出版信息
Biochem Biophys Res Commun. 2009 Jan 16;378(3):513-7. doi: 10.1016/j.bbrc.2008.11.072. Epub 2008 Nov 28.
SUMOylation regulates a variety of cellular processes, including control of transcriptional activities of nuclear receptors. Here, we present SUMOylation of orphan nuclear receptor, RORalpha by both SUMO-1 and SUMO-2. SUMOylation of RORalpha occurred on the 240th lysine residue at the hinge region of human protein. PIAS family members, PIASxalpha, PIAS3, and PIASy, increased SUMOylation of RORalpha, whereas SENP2 specifically removed SUMO from RORalpha. SUMOylation-defective mutant form of RORalpha exhibited decreased transcriptional activity on RORalpha-responsive promoters indicating that SUMOylation may positively regulate transcriptional function of RORalpha.
SUMO化修饰调控多种细胞过程，包括对核受体转录活性的控制。在此，我们展示了孤儿核受体RORα可被SUMO-1和SUMO-2进行SUMO化修饰。RORα的SUMO化修饰发生在人源蛋白铰链区的第240位赖氨酸残基上。PIAS家族成员PIASxα、PIAS3和PIASy可增强RORα的SUMO化修饰，而SENP2则特异性地去除RORα上的SUMO。RORα的SUMO化缺陷突变体形式在RORα反应性启动子上表现出转录活性降低，这表明SUMO化修饰可能正向调节RORα的转录功能。
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