KCNE5 induces time- and voltage-dependent modulation of the KCNQ1 current.

Research output: Contribution to journalJournal article

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KCNE5 induces time- and voltage-dependent modulation of the KCNQ1 current. / Angelo, Kamilla; Jespersen, Thomas; Grunnet, Morten; Nielsen, Morten Schak; Klaerke, Dan A; Olesen, Søren-Peter.

In: Biophysical Journal, Vol. 83, No. 4, 2002, p. 1997-2006.

Research output: Contribution to journalJournal article

Harvard

Angelo, K, Jespersen, T, Grunnet, M, Nielsen, MS, Klaerke, DA & Olesen, S-P 2002, 'KCNE5 induces time- and voltage-dependent modulation of the KCNQ1 current.', Biophysical Journal, vol. 83, no. 4, pp. 1997-2006.

APA

Angelo, K., Jespersen, T., Grunnet, M., Nielsen, M. S., Klaerke, D. A., & Olesen, S-P. (2002). KCNE5 induces time- and voltage-dependent modulation of the KCNQ1 current. Biophysical Journal, 83(4), 1997-2006.

Vancouver

Angelo K, Jespersen T, Grunnet M, Nielsen MS, Klaerke DA, Olesen S-P. KCNE5 induces time- and voltage-dependent modulation of the KCNQ1 current. Biophysical Journal. 2002;83(4):1997-2006.

Author

Angelo, Kamilla ; Jespersen, Thomas ; Grunnet, Morten ; Nielsen, Morten Schak ; Klaerke, Dan A ; Olesen, Søren-Peter. / KCNE5 induces time- and voltage-dependent modulation of the KCNQ1 current. In: Biophysical Journal. 2002 ; Vol. 83, No. 4. pp. 1997-2006.

Bibtex

@article{b3da9740ab5511ddb5e9000ea68e967b,
title = "KCNE5 induces time- and voltage-dependent modulation of the KCNQ1 current.",
abstract = "The function of the KCNE5 (KCNE1-like) protein has not previously been described. Here we show that KCNE5 induces both a time- and voltage-dependent modulation of the KCNQ1 current. Interaction of the KCNQ1 channel with KCNE5 shifted the voltage activation curve of KCNQ1 by more than 140 mV in the positive direction. The activation threshold of the KCNQ1+KCNE5 complex was +40 mV and the midpoint of activation was +116 mV. The KCNQ1+KCNE5 current activated slowly and deactivated rapidly as compared to the KCNQ1+KCNE1 at 22 degrees C; however, at physiological temperature, the activation time constant of the KCNQ1+KCNE5 current decreased fivefold, thus exceeding the activation rate of the KCNQ1+KCNE1 current. The KCNE5 subunit is specific for the KCNQ1 channel, as none of other members of the KCNQ-family or the human ether a-go-go related channel (hERG1) was affected by KCNE5. Four residues in the transmembrane domain of the KCNE5 protein were found to be important for the control of the voltage-dependent activation of the KCNQ1 current. We speculate that since KCNE5 is expressed in cardiac tissue it may here along with the KCNE1 beta-subunit regulate KCNQ1 channels. It is possible that KCNE5 shapes the I(Ks) current in certain parts of the mammalian heart.",
author = "Kamilla Angelo and Thomas Jespersen and Morten Grunnet and Nielsen, {Morten Schak} and Klaerke, {Dan A} and S{\o}ren-Peter Olesen",
note = "Keywords: Action Potentials; Amino Acid Sequence; Animals; Biophysics; CHO Cells; Cricetinae; Electrophysiology; Ions; KCNQ Potassium Channels; KCNQ1 Potassium Channel; Kinetics; Molecular Sequence Data; Potassium Channels; Potassium Channels, Voltage-Gated; Protein Structure, Tertiary; Temperature; Time Factors; Xenopus laevis",
year = "2002",
language = "English",
volume = "83",
pages = "1997--2006",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - KCNE5 induces time- and voltage-dependent modulation of the KCNQ1 current.

AU - Angelo, Kamilla

AU - Jespersen, Thomas

AU - Grunnet, Morten

AU - Nielsen, Morten Schak

AU - Klaerke, Dan A

AU - Olesen, Søren-Peter

N1 - Keywords: Action Potentials; Amino Acid Sequence; Animals; Biophysics; CHO Cells; Cricetinae; Electrophysiology; Ions; KCNQ Potassium Channels; KCNQ1 Potassium Channel; Kinetics; Molecular Sequence Data; Potassium Channels; Potassium Channels, Voltage-Gated; Protein Structure, Tertiary; Temperature; Time Factors; Xenopus laevis

PY - 2002

Y1 - 2002

N2 - The function of the KCNE5 (KCNE1-like) protein has not previously been described. Here we show that KCNE5 induces both a time- and voltage-dependent modulation of the KCNQ1 current. Interaction of the KCNQ1 channel with KCNE5 shifted the voltage activation curve of KCNQ1 by more than 140 mV in the positive direction. The activation threshold of the KCNQ1+KCNE5 complex was +40 mV and the midpoint of activation was +116 mV. The KCNQ1+KCNE5 current activated slowly and deactivated rapidly as compared to the KCNQ1+KCNE1 at 22 degrees C; however, at physiological temperature, the activation time constant of the KCNQ1+KCNE5 current decreased fivefold, thus exceeding the activation rate of the KCNQ1+KCNE1 current. The KCNE5 subunit is specific for the KCNQ1 channel, as none of other members of the KCNQ-family or the human ether a-go-go related channel (hERG1) was affected by KCNE5. Four residues in the transmembrane domain of the KCNE5 protein were found to be important for the control of the voltage-dependent activation of the KCNQ1 current. We speculate that since KCNE5 is expressed in cardiac tissue it may here along with the KCNE1 beta-subunit regulate KCNQ1 channels. It is possible that KCNE5 shapes the I(Ks) current in certain parts of the mammalian heart.

AB - The function of the KCNE5 (KCNE1-like) protein has not previously been described. Here we show that KCNE5 induces both a time- and voltage-dependent modulation of the KCNQ1 current. Interaction of the KCNQ1 channel with KCNE5 shifted the voltage activation curve of KCNQ1 by more than 140 mV in the positive direction. The activation threshold of the KCNQ1+KCNE5 complex was +40 mV and the midpoint of activation was +116 mV. The KCNQ1+KCNE5 current activated slowly and deactivated rapidly as compared to the KCNQ1+KCNE1 at 22 degrees C; however, at physiological temperature, the activation time constant of the KCNQ1+KCNE5 current decreased fivefold, thus exceeding the activation rate of the KCNQ1+KCNE1 current. The KCNE5 subunit is specific for the KCNQ1 channel, as none of other members of the KCNQ-family or the human ether a-go-go related channel (hERG1) was affected by KCNE5. Four residues in the transmembrane domain of the KCNE5 protein were found to be important for the control of the voltage-dependent activation of the KCNQ1 current. We speculate that since KCNE5 is expressed in cardiac tissue it may here along with the KCNE1 beta-subunit regulate KCNQ1 channels. It is possible that KCNE5 shapes the I(Ks) current in certain parts of the mammalian heart.

M3 - Journal article

C2 - 12324418

VL - 83

SP - 1997

EP - 2006

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 4

ER -

ID: 8419063