鈉離子通道S4/D1與S4/D4區段與
通道活化及不活化反應之關係

舒馨慧

doi:10.6342/NTU.2006.01912

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鈉離子通道S4/D1與S4/D4區段與通道活化及不活化反應之關係

The Different Roles of S4/D1 and S4/D4 Segments in Sodium Channel Activation and Inactivation

舒馨慧 , Masters　　Advisor：郭鐘金　　

繁體中文 DOI： 10.6342/NTU.2006.01912

鈉離子通道；第四結構區域；第一結構區域；第四穿膜區段； sodium channel ； D4 ； D1 ； S4

Abstract │ Reference (92) │ Altmetrics

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Abstract

Rat brain type IIA Na+ channel is a member of the voltage-gated Na+ channel which is composed of four structurally similar domains (I-IV). Each of the domain has six transmembrane segments (S1-S6). Because S4 contains regularly spaced basic amino acids, it has been considered as the voltage sensor of the channel. S4 presumably moves in response to membrane electric field change, leading into different gating conformations of the channel. There are chiefly two models explaining the S4 movement: the helical screw (S4 move translationally and rotationally in a gating canal which is composed of part of the channel protein), and the paddle model (S4 lying at the channel periphery and moving as one unit with S3b). Among the four S4s, the one in domain 4 (S4/D4) is especially implicated in Na+ channel inactivation and has been shown to move externally upon membrane depolarization. The amino acids in S3-4 linker and S4 are devided into three axes: the positive basic residues in S4 are called the “R” axis, extending to the hydrophobic residues in S3-4 linker ; the hydrophobic residues ahead of the “R” axis are called the “R-1” axis, and the next ones are the “R+1” axis. We made point mutations of the uncharged residues into arginine in the S3-4 linker and S4, and used two-electrode voltage clamp technique to study the effect of the mutation on channel gating. We found that many arginine mutations on S3-4 linker of domain one and domain four produced negative (hyperpolarized) shifts of the activation curve or inactivation curve, especially in the “R-1” axis, suggesting the essential role of this axis in stabilizing the channel in the resting state. The “impedance zone” surrounding S4 is surprisingly much wider in the Na+ channel than in the Shaker K+ channel. However, it seems plausible that like the S4 in the Shaker channel, the S4 in the Na+ channel are likely to move ~9 residues with a rotation of ~180° during channel activation/inactivation. According to the results of mutations of S3-4 linker at the position just preceding R1, we considered that different domains play different roles during channel activation/inactivation: domain four plays an important role only in channel inactivation, and domain one very likely is involved primarily in channel activation.

Reference ( 92 ) 〈TOP〉

Aggarwal, S. K., and MacKinnon, R.(1996). Contribution of the S4 segment to gating charge in the Shaker K+ channel. Neuron 16, 1169-1177.
連結：
Ahern, C.A., and Horn, R. (2004). Specificity of charge-carrying residues in the voltage sensor of potassium channels. J. Gen. Physiol.123, 205–216.
連結：
Ahern, C.A., and Horn, R. (2005).Focused electric field across the voltage sensor of potassium channels. Neuron 48,25-29.
連結：
Armstrong, C.M. (1981). Sodium channels and gating currents. Physiol. Rev. 61, 644–682.
連結：
Backx, P.H., D.T. Yue, J.H. Lawrence, E. Marban, and G.F. Tomaselli. (1992) Molecular localization of an ion-binding site within the pore of mammalian sodium channels. Science (Wash. DC). 257:248–251.
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