Transmembrane movement of the Shaker K+ channel S4
Transmembrane movement of the Shaker K+ channel S4
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DOI:
10.1016/s0896-6273(00)80056-2
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发表时间:
1996-02-01
期刊:
影响因子:
16.2
通讯作者:
Isacoff, EY
中科院分区:
文献类型:
--
作者:
Larsson, HP;Baker, OS;Isacoff, EY
We have probed internal and external accessibility of S4 residues to the membrane-impermeant thiol reagent methanethiosulfonate-ethyltrimethylammonium (MTSET) in both open and closed, cysteine-substituted Shaker K+ channels. Our results indicate that S4 traverses the membrane with no more than 5 amino acids in the closed state, and that the distribution of buried residues changes when channels open. This change argues for a displacement of S4 through the plane of the membrane in which an initially intracellular residue moves to within 3 amino acids of the extracellular solution. These results demonstrate that the putative voltage-sensing charges of S4 actually reside in the membrane and that they move outward when channels open. We consider constraints placed on channel structure by these results.