Schopperle W M, Holmqvist M H, Zhou Y, Wang J, Wang Z, Griffith L C, Keselman I, Kusinitz F, Dagan D, Levitan I B
Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254, USA.
Neuron. 1998 Mar;20(3):565-73. doi: 10.1016/s0896-6273(00)80995-2.
Slob, a novel protein that binds to the carboxy-terminal domain of the Drosophila Slowpoke (dSlo) calcium-dependent potassium channel, was identified with a yeast two-hybrid screen. Slob and dSlo coimmunoprecipitate from Drosophila heads and heterologous host cells, suggesting that they interact in vivo. Slob also coimmunoprecipitates with the Drosophila EAG potassium channel but not with Drosophila Shaker, mouse Slowpoke, or rat Kv1.3. Confocal fluorescence microscopy demonstrates that Slob and dSlo redistribute in cotransfected cells and are colocalized in large intracellular structures. Direct application of Slob to the cytoplasmic face of detached membrane patches containing dSlo channels leads to an increase in channel activity. Slob may represent a new class of multi-functional channel-binding proteins.
通过酵母双杂交筛选鉴定出一种名为Slob的新型蛋白质，它可与果蝇Slowpoke（dSlo）钙依赖性钾通道的羧基末端结构域结合。Slob和dSlo可从果蝇头部和异源宿主细胞中共免疫沉淀，这表明它们在体内相互作用。Slob也可与果蝇EAG钾通道共免疫沉淀，但不能与果蝇Shaker、小鼠Slowpoke或大鼠Kv1.3共免疫沉淀。共聚焦荧光显微镜显示，Slob和dSlo在共转染细胞中重新分布，并在大型细胞内结构中共定位。将Slob直接应用于含有dSlo通道的分离膜片的细胞质面会导致通道活性增加。Slob可能代表一类新型的多功能通道结合蛋白。
