Voltage Gating of Shaker K+ Channels
نویسندگان
چکیده
منابع مشابه
Voltage Gating of Shaker K+ Channels
Ionic (Ii) and gating currents (Ig) from noninactivating Shaker H4 K+ channels were recorded with the cut-open oocyte voltage clamp and macropatch techniques. Steady state and kinetic properties were studied in the temperature range 2-22 degreesC. The time course of Ii elicited by large depolarizations consists of an initial delay followed by an exponential rise with two kinetic components. The...
متن کاملExtent of Voltage Sensor Movement during Gating of Shaker K+ Channels
Voltage-driven activation of Kv channels results from conformational changes of four voltage sensor domains (VSDs) that surround the K(+) selective pore domain. How the VSD helices rearrange during gating is an area of active research. Luminescence resonance energy transfer (LRET) is a powerful spectroscopic ruler uniquely suitable for addressing the conformational trajectory of these helices. ...
متن کاملA role for hydrophobic residues in the voltage-dependent gating of Shaker K+ channels.
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...
متن کاملTaking Apart the Gating of Voltage-Gated K+ Channels
؉ Channels labeling studies of KcsA suggest that K ϩ channels may gate by rotating the inner helices that line the pore (Per-ozo et al., 1999). In this model, the degree of rotation of the helices regulates the aperture of the inner mouth of the pore that opens and closes like the shutters of a San Francisco, California 94143 camera. For voltage-gated K ϩ channels, this model is broadly consist...
متن کاملVoltage-insensitive Gating after Charge-neutralizing Mutations in the S4 Segment of Shaker Channels
Shaker channel mutants, in which the first (R362), second (R365), and fourth (R371) basic residues in the S4 segment have been neutralized, are found to pass potassium currents with voltage-insensitive kinetics when expressed in Xenopus oocytes. Single channel recordings clarify that these channels continue to open and close from -160 to +80 mV with a constant opening probability (Po). Although...
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ژورنال
عنوان ژورنال: Journal of General Physiology
سال: 1998
ISSN: 0022-1295,1540-7748
DOI: 10.1085/jgp.112.2.223