Busch A E, Suessbrich H
Max-Planck-Institut für experimentelle Medizin, Göttingen, Germany.
Trends Pharmacol Sci. 1997 Jan;18(1):26-9. doi: 10.1016/s0165-6147(96)01016-4.
The ISK (also called minK) protein, although it is structurally unrelated to any other ion channel subunit, induces slowly activating, voltage-dependent K+ channels (IminK) in Xenopus oocytes or HEK293 cells. The quaternary structure of the IminK channel complex has long remained a mystery, but recent studies suggest an interaction of the ISK protein with a traditional K+ channel subunit, identified in man as KVLQT1. It is unclear at this point what the mechanism of this interaction is, or whether the ISK protein may also interact with other ion channel subunits. However, there is an abundance of information regarding the role and regulation of the ISK protein in the IminK channel complex, discussed in this review by Andreas Busch and Hartmut Suessbrich. The ISK protein is expressed in different tissues, where IminK activation may have distinct net effects on cell function. This fact makes IminK an excellent target for pharmacological agents.
ISK(也称为minK)蛋白,尽管其在结构上与任何其他离子通道亚基均无关联,但在非洲爪蟾卵母细胞或人胚肾293(HEK293)细胞中可诱导缓慢激活的电压依赖性钾通道(IminK)。长期以来,IminK通道复合体的四级结构一直是个谜,但最近的研究表明,ISK蛋白与一种传统的钾通道亚基存在相互作用,在人类中该亚基被鉴定为KVLQT1。目前尚不清楚这种相互作用的机制是什么,也不清楚ISK蛋白是否还可能与其他离子通道亚基相互作用。然而,关于ISK蛋白在IminK通道复合体中的作用和调节有大量信息,安德烈亚斯·布施和哈特穆特·叙斯布里希在本综述中对此进行了讨论。ISK蛋白在不同组织中表达,IminK的激活可能对细胞功能产生不同的净效应。这一事实使得IminK成为药物的理想靶点。