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Article

Hydrophobic substitution mutations in the S4 sequence alter voltage-dependent gating in Shaker K+ channels.

Neuron - 1 Aug 1991

Lopez G A, Jan Y N, Jan L Y

Abstract excerpt

Voltage-activated Na+, Ca2+, and K+ channels contain a common motif, the S4 sequence, characterized by a basic residue at every third position interspersed mainly with hydrophobic residues. The S4 sequence is proposed to function as the voltage sensor and to move in response to membrane depolarization, triggering conformational changes that open the channel. This hypothesis has been tested in previous studies...

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Source

Identifiers

PMID: 1873032
DOI: 10.1016/0896-6273(91)90271-z

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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Hydrophobic substitution mutations in the S4 sequence alter voltage-dependent gating in Shaker K+ channels.PMID 1873032Read ↗

Role of hydrophobic and ionic forces in the movement of S4 of the Shaker potassium channel.Semantic proximity Read ↗

S4 mutations alter the single-channel gating kinetics of Shaker K+ channels.Semantic proximity Read ↗

Contribution of the central hydrophobic residue in the PXP motif of voltage-dependent K+ channels to S6 flexibility and gating properties.Semantic proximity Read ↗

Mutations in the S6 gate isolate a late step in the activation pathway and reduce 4-AP sensitivity in shaker K(v) channel.Semantic proximity Read ↗

Non-native R1 substitution in the s4 domain uniquely alters Kv4.3 channel gating.Semantic proximity Read ↗

Gating of shaker-type channels requires the flexibility of S6 caused by prolines.Semantic proximity Read ↗

The isolated voltage sensing domain of the Shaker potassium channel forms a voltage-gated cation channel.Semantic proximity Read ↗

Nonsensing residues in S3-S4 linker's C terminus affect the voltage sensor set point in K+ channels.Semantic proximity Read ↗

Voltage-insensitive gating after charge-neutralizing mutations in the S4 segment of Shaker channels.Semantic proximity Read ↗

A characterization of the activating structural rearrangements in voltage-dependent Shaker K+ channels.Semantic proximity Read ↗

Atomic proximity between S4 segment and pore domain in Shaker potassium channels.Semantic proximity Read ↗

Localization of the extracellular end of the voltage sensor S4 in a potassium channel.Semantic proximity Read ↗

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