Sewing S, Roeper J, Pongs O
Zentrum für Molekulare Neurobiologie Institut für Neurale Signalverarbeitung, Hamburg Federal Republic of Germany.
Neuron. 1996 Feb;16(2):455-63. doi: 10.1016/s0896-6273(00)80063-x.
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 aminoterminal 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.
来自哺乳动物大脑的电压激活钾(Kv)通道是包含α和β亚基的异源寡聚体。在体外表达系统中,Kv1α和Kvβ1亚基的共表达赋予非失活钾通道(延迟整流器)快速A型失活特性。我们已经确定了Kv1.5氨基末端长达90个氨基酸(第112 - 201位残基)的区域,该区域足以实现Kv1.5α和Kvβ1亚基的相互作用。在Kv1.5氨基末端的这个区域内(第193 - 201位残基),检测到一个Kvβ1相互作用位点,它是Kvβ1介导的Kv1.5电流快速失活所必需的。这种相互作用位点基序(FYE/QLGE/DEAM/L)仅在与Shaker相关的亚家族(Kv1)中发现。结果表明,α亚基和Kvβ1亚基之间的异源寡聚化仅限于与Shaker相关的钾通道α亚基。