Vastiau Annick, Cao Lishuang, Jaspers Martine, Owsianik Grzegorz, Janssens Veerle, Cuppens Harry, Goris Jozef, Nilius Bernd, Cassiman Jean-Jacques
Department of Human Genetics, Division of Human Mutations and Polymorphisms, KULeuven, Herestraat 49, Postbus 602, 3000 Leuven, Belgium.
FEBS Lett. 2005 Jun 20;579(16):3392-6. doi: 10.1016/j.febslet.2005.04.079.
A direct interaction of the regulatory domain (R domain) of the cystic fibrosis transmembrane conductance regulator protein (CFTR) with PR65, a regulatory subunit of the protein phosphatase 2A (PP2A), was shown in yeast two hybrid, pull-down and co-immunoprecipitation experiments. The R domain could be dephosphorylated by PP2A in vitro. Overexpression of the interacting domain of PR65 in Caco-2 cells, as well as treatment with okadaic acid, showed a prolonged deactivation of the chloride channel. Taken together our results show a direct and functional interaction between CFTR and PP2A.
酵母双杂交、下拉和免疫共沉淀实验表明，囊性纤维化跨膜传导调节蛋白（CFTR）的调节结构域（R结构域）与蛋白磷酸酶2A（PP2A）的调节亚基PR65存在直接相互作用。R结构域在体外可被PP2A去磷酸化。在Caco-2细胞中过表达PR65的相互作用结构域以及用冈田酸处理，均显示氯离子通道的失活时间延长。综合我们的结果表明，CFTR与PP2A之间存在直接的功能相互作用。
