Kv beta 1 subunit binding specific for Shaker-related potassium channel alpha subunits
Kv beta 1 subunit binding specific for Shaker-related potassium channel alpha subunits
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DOI：
10.1016/s0896-6273(00)80063-x
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发表时间：
1996-02-01
期刊：
影响因子：
16.2
通讯作者：
Pongs, O
中科院分区：
文献类型：
--
作者：
Sewing, S;Roeper, J;Pongs, O
来自哺乳动物脑的电压激活钾（Kv）通道是含有α和β亚基的异源寡聚体。Kv 1 α和Kv β 1亚基的共表达在体外表达系统中赋予非失活钾通道（延迟整流器）快速A型失活。我们已经描绘了一个Kv1.5氨基末端区域的多达90个氨基酸（残基112-201），这是足够的Kv1.5 α和Kv β 1亚基的相互作用。在Kv1.5氨基末端（残基193-201）的该区域内，检测到Kv β 1介导的Kv1.5电流快速失活所必需的Kv β 1相互作用位点。这种相互作用位点基序（FYE/QLGE/DEAM/L）仅在Shaker相关亚家族（Kv 1）中发现。结果表明，α和Kv β 1亚基之间的异源寡聚化仅限于Shaker相关的钾通道α亚基。
Voltage-activated potassium (Kv) channels from mammalian brain are hetero-oligomers containing alpha and beta subunits. Coexpression of Kv1 alpha and Kv beta 1 subunits confers rapid A-type inactivation on noninactivating potassium channels (delayed rectifiers) in expression systems in vitro. We have delineated a Kv1.5 amino-terminal region of up to 90 amino acids (residues 112-201) that is sufficient for interactions of Kv1.5 alpha and Kv beta 1 subunits. Within this region of the Kv1.5 amino terminus (residues 193-201), a Kv beta 1 interaction site necessary for Kv beta 1-mediated rapid inactivation of Kv1.5 currents was detected. This interaction site motif (FYE/QLGE/DEAM/L) is found exclusively in the Shaker-related subfamily (Kv1). The results show that hetero-oligomerization between alpha and Kv beta 1 subunits is restricted to Shaker-related potassium channel alpha subunits.