Exploring the architecture of potassium channels using chimeras to reveal signal transduction

Baron Chanda; J. K. Tiwari; Anurag Varshney; M. K. Mathew

doi:10.1023/A:1020550408733

Exploring the architecture of potassium channels using chimeras to reveal signal transduction

Baron Chanda
, J. K. Tiwari
, Anurag Varshney
, M. K. Mathew

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

The chimaeric channel, 4N/1, generated from two outwardly rectifying K⁺ channels by linking the N-terminal cytoplasmic domain of hKv1.4 with the transmembrane body of hKv1.1, functions as an inward rectifier. The operating range of the channel is shifted to hyperpolarizing potentials and it is inactivated at resting membrane potentials. Coexpression of a truncated form of hKv1.1 with the N-terminal domain of hKv1.4 results in the same physiology as the chimera implying specific interactions between the two segments.

Original language	English
Pages (from-to)	301-306
Number of pages	6
Journal	Bioscience Reports
Volume	19
Issue number	4
DOIs	https://doi.org/10.1023/A:1020550408733
State	Published - 1999

Keywords

Chimaera
Ion channel
Ion selectivity
Voltage sensing

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abstract = "The chimaeric channel, 4N/1, generated from two outwardly rectifying K+ channels by linking the N-terminal cytoplasmic domain of hKv1.4 with the transmembrane body of hKv1.1, functions as an inward rectifier. The operating range of the channel is shifted to hyperpolarizing potentials and it is inactivated at resting membrane potentials. Coexpression of a truncated form of hKv1.1 with the N-terminal domain of hKv1.4 results in the same physiology as the chimera implying specific interactions between the two segments.",

keywords = "Chimaera, Ion channel, Ion selectivity, Voltage sensing",

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AU - Chanda, Baron

AU - Tiwari, J. K.

AU - Varshney, Anurag

AU - Mathew, M. K.

PY - 1999

Y1 - 1999

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AB - The chimaeric channel, 4N/1, generated from two outwardly rectifying K+ channels by linking the N-terminal cytoplasmic domain of hKv1.4 with the transmembrane body of hKv1.1, functions as an inward rectifier. The operating range of the channel is shifted to hyperpolarizing potentials and it is inactivated at resting membrane potentials. Coexpression of a truncated form of hKv1.1 with the N-terminal domain of hKv1.4 results in the same physiology as the chimera implying specific interactions between the two segments.

KW - Chimaera

KW - Ion channel

KW - Ion selectivity

KW - Voltage sensing

UR - https://www.scopus.com/pages/publications/0032694384

U2 - 10.1023/A:1020550408733

DO - 10.1023/A:1020550408733

M3 - Article

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VL - 19

SP - 301

EP - 306

JO - Bioscience Reports

JF - Bioscience Reports

IS - 4

ER -

Exploring the architecture of potassium channels using chimeras to reveal signal transduction

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Keywords

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