疏水残基在Shaker钾离子通道电压依赖性门控中的作用。
A role for hydrophobic residues in the voltage-dependent gating of Shaker K+ channels.
作者信息
McCormack K, Tanouye M A, Iverson L E, Lin J W, Ramaswami M, McCormack T, Campanelli J T, Mathew M K, Rudy B
机构信息
Division of Biology 216-76, California Institute of Technology, Pasadena 91125.
出版信息
Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2931-5. doi: 10.1073/pnas.88.7.2931.
Abstract
A leucine heptad repeat is well conserved in voltage-dependent ion channels. Herein we examine the role of the repeat region in Shaker K+ channels through substitution of the leucines in the repeat and through coexpression of normal and truncated products. In contrast to leucine-zipper DNA-binding proteins, we find that the subunit assembly of Shaker does not depend on the leucine heptad repeat. Instead, we report that substitutions of the leucines in the repeat produce large effects on the observed voltage dependence of conductance voltage and prepulse inactivation curves. Our results suggest that the leucines mediate interactions that play an important role in the transduction of charge movement into channel opening and closing.
摘要
亮氨酸七肽重复序列在电压依赖性离子通道中高度保守。在此，我们通过替换重复序列中的亮氨酸以及共表达正常和截短产物，研究了重复区域在Shaker钾通道中的作用。与亮氨酸拉链DNA结合蛋白不同，我们发现Shaker的亚基组装不依赖于亮氨酸七肽重复序列。相反，我们报告重复序列中亮氨酸的替换对观察到的电导电压和预脉冲失活曲线的电压依赖性产生了很大影响。我们的结果表明，亮氨酸介导的相互作用在将电荷运动转化为通道开闭的过程中起着重要作用。
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