Shan Shi-Fang, Wang Lin-Fang, Zhai Jian-Wei, Qin Yi, Ouyang Hua-Fang, Kong Yu-Ying, Liu Jing, Wang Yuan, Xie You-Hua
Institute of Biochemistry and Cell Biology, Shanghai Institutes of Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
FEBS Lett. 2008 Nov 12;582(27):3723-8. doi: 10.1016/j.febslet.2008.09.057. Epub 2008 Oct 21.
Prospero-related homeobox protein (Prox1) plays essential roles in the development of many tissues and organs. In the present study, we show that Prox1 is modified by the small ubiquitin-like protein SUMO-1 in cultured cells. Mutation analysis identified at least four potential sumoylation sites within the repression domain of Prox1. Our data indicate that sumoylation of Prox1 reduces its interaction with HDAC3 and as a result downregulates its corepressor activity. These findings suggest that sumoylation may serve as a novel mechanism for the regulation of Prox1's corepressor activity.
与Prospero相关的同源盒蛋白（Prox1）在许多组织和器官的发育中起着至关重要的作用。在本研究中，我们发现Prox1在培养细胞中被小泛素样蛋白SUMO-1修饰。突变分析确定了Prox1抑制域内至少四个潜在的SUMO化位点。我们的数据表明，Prox1的SUMO化减少了其与HDAC3的相互作用，从而下调了其共抑制因子活性。这些发现表明，SUMO化可能是调节Prox1共抑制因子活性的一种新机制。
