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A single amino acid mutation attenuates rundown of voltage-gated calcium channels

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.febslet.2006.09.027 Byline: Xiao-Guang Zhen, Cheng Xie, Yoichi Yamada, Yun Zhang, Christina Doyle, Jian Yang Keywords: P/Q-type calcium channels; Rundown; PIP.sub.2; Inside-out patch; Mutagenesis; S6 Abstract:... Full description

Journal Title: FEBS Letters Oct 16, 2006, Vol.580(24), p.5733(6)
Main Author: Zhen, Xiao - Guang
Other Authors: Xie, Cheng , Yamada, Yoichi , Zhang, Yun , Doyle, Christina , Yang, Jian
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0014-5793
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recordid: gale_ofa196254533
title: A single amino acid mutation attenuates rundown of voltage-gated calcium channels
format: Article
creator:
  • Zhen, Xiao - Guang
  • Xie, Cheng
  • Yamada, Yoichi
  • Zhang, Yun
  • Doyle, Christina
  • Yang, Jian
subjects:
  • Aspartate -- Genetic Aspects
  • Phosphatidylinositols -- Genetic Aspects
  • Calcium Channels -- Genetic Aspects
  • Histidine -- Genetic Aspects
ispartof: FEBS Letters, Oct 16, 2006, Vol.580(24), p.5733(6)
description: To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.febslet.2006.09.027 Byline: Xiao-Guang Zhen, Cheng Xie, Yoichi Yamada, Yun Zhang, Christina Doyle, Jian Yang Keywords: P/Q-type calcium channels; Rundown; PIP.sub.2; Inside-out patch; Mutagenesis; S6 Abstract: The activity of voltage-gated calcium channels (VGCCs) decreases with time in whole-cell and inside-out patch-clamp recordings. In this study we found that substituting a single amino acid (I1520) at the intracellular end of IIIS6 in the [alpha].sub.1 subunit of P/Q-type Ca.sup.2+ channels with histidine or aspartate greatly attenuated channel rundown in inside-out patch-clamp recordings. The homologous mutations also slowed rundown of N- and L-type Ca.sup.2+ channels, albeit to a lesser degree. In P/Q-type channels, the attenuation of rundown is accompanied by an increased apparent affinity for phosphatidylinositol-4,5-bisphosphate, which has been shown to be critical for maintaining Ca.sup.2+ channel activity [L. Wu, C.S. Bauer, X.-G. Zhen, C. Xie, J. Yang, Dual regulation of voltage-gated calcium channels by PtdIns(4,5)P2. Nature 419 (2002) 947-952]. Furthermore, the histidine mutation significantly stabilized the open state, making the channels easier to open, slower to close, harder to inactivate and faster to recover from inactivation. Our finding that mutation of a single amino acid can greatly attenuate rundown provides an easy and efficient way to slow the rundown of VGCCs, facilitating functional studies that require direct access to the cytoplasmic side of the channel. Author Affiliation: Department of Biological Sciences, 917 Fairchild Center, MC2462, Columbia University, New York, NY 10027, USA Article History: Received 31 July 2006; Revised 6 September 2006; Accepted 13 September 2006
language: English
source:
identifier: ISSN: 0014-5793
fulltext: fulltext
issn:
  • 0014-5793
  • 00145793
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titleA single amino acid mutation attenuates rundown of voltage-gated calcium channels
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ispartofFEBS Letters, Oct 16, 2006, Vol.580(24), p.5733(6)
identifierISSN: 0014-5793
subjectAspartate -- Genetic Aspects ; Phosphatidylinositols -- Genetic Aspects ; Calcium Channels -- Genetic Aspects ; Histidine -- Genetic Aspects
descriptionTo link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.febslet.2006.09.027 Byline: Xiao-Guang Zhen, Cheng Xie, Yoichi Yamada, Yun Zhang, Christina Doyle, Jian Yang Keywords: P/Q-type calcium channels; Rundown; PIP.sub.2; Inside-out patch; Mutagenesis; S6 Abstract: The activity of voltage-gated calcium channels (VGCCs) decreases with time in whole-cell and inside-out patch-clamp recordings. In this study we found that substituting a single amino acid (I1520) at the intracellular end of IIIS6 in the [alpha].sub.1 subunit of P/Q-type Ca.sup.2+ channels with histidine or aspartate greatly attenuated channel rundown in inside-out patch-clamp recordings. The homologous mutations also slowed rundown of N- and L-type Ca.sup.2+ channels, albeit to a lesser degree. In P/Q-type channels, the attenuation of rundown is accompanied by an increased apparent affinity for phosphatidylinositol-4,5-bisphosphate, which has been shown to be critical for maintaining Ca.sup.2+ channel activity [L. Wu, C.S. Bauer, X.-G. Zhen, C. Xie, J. Yang, Dual regulation of voltage-gated calcium channels by PtdIns(4,5)P2. Nature 419 (2002) 947-952]. Furthermore, the histidine mutation significantly stabilized the open state, making the channels easier to open, slower to close, harder to inactivate and faster to recover from inactivation. Our finding that mutation of a single amino acid can greatly attenuate rundown provides an easy and efficient way to slow the rundown of VGCCs, facilitating functional studies that require direct access to the cytoplasmic side of the channel. Author Affiliation: Department of Biological Sciences, 917 Fairchild Center, MC2462, Columbia University, New York, NY 10027, USA Article History: Received 31 July 2006; Revised 6 September 2006; Accepted 13 September 2006
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titleA single amino acid mutation attenuates rundown of voltage-gated calcium channels.
descriptionTo link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.febslet.2006.09.027 Byline: Xiao-Guang Zhen, Cheng Xie, Yoichi Yamada, Yun Zhang, Christina Doyle, Jian Yang Keywords: P/Q-type calcium channels; Rundown; PIP.sub.2; Inside-out patch; Mutagenesis; S6 Abstract: The activity of voltage-gated calcium channels (VGCCs) decreases with time in whole-cell and inside-out patch-clamp recordings. In this study we found that substituting a single amino acid (I1520) at the intracellular end of IIIS6 in the [alpha].sub.1 subunit of P/Q-type Ca.sup.2+ channels with histidine or aspartate greatly attenuated channel rundown in inside-out patch-clamp recordings. The homologous mutations also slowed rundown of N- and L-type Ca.sup.2+ channels, albeit to a lesser degree. In P/Q-type channels, the attenuation of rundown is accompanied by an increased apparent affinity for phosphatidylinositol-4,5-bisphosphate, which has been shown to be critical for maintaining Ca.sup.2+ channel activity [L. Wu, C.S. Bauer, X.-G. Zhen, C. Xie, J. Yang, Dual regulation of voltage-gated calcium channels by PtdIns(4,5)P2. Nature 419 (2002) 947-952]. Furthermore, the histidine mutation significantly stabilized the open state, making the channels easier to open, slower to close, harder to inactivate and faster to recover from inactivation. Our finding that mutation of a single amino acid can greatly attenuate rundown provides an easy and efficient way to slow the rundown of VGCCs, facilitating functional studies that require direct access to the cytoplasmic side of the channel. Author Affiliation: Department of Biological Sciences, 917 Fairchild Center, MC2462, Columbia University, New York, NY 10027, USA Article History: Received 31 July 2006; Revised 6 September 2006; Accepted 13 September 2006
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abstractTo link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.febslet.2006.09.027 Byline: Xiao-Guang Zhen, Cheng Xie, Yoichi Yamada, Yun Zhang, Christina Doyle, Jian Yang Keywords: P/Q-type calcium channels; Rundown; PIP.sub.2; Inside-out patch; Mutagenesis; S6 Abstract: The activity of voltage-gated calcium channels (VGCCs) decreases with time in whole-cell and inside-out patch-clamp recordings. In this study we found that substituting a single amino acid (I1520) at the intracellular end of IIIS6 in the [alpha].sub.1 subunit of P/Q-type Ca.sup.2+ channels with histidine or aspartate greatly attenuated channel rundown in inside-out patch-clamp recordings. The homologous mutations also slowed rundown of N- and L-type Ca.sup.2+ channels, albeit to a lesser degree. In P/Q-type channels, the attenuation of rundown is accompanied by an increased apparent affinity for phosphatidylinositol-4,5-bisphosphate, which has been shown to be critical for maintaining Ca.sup.2+ channel activity [L. Wu, C.S. Bauer, X.-G. Zhen, C. Xie, J. Yang, Dual regulation of voltage-gated calcium channels by PtdIns(4,5)P2. Nature 419 (2002) 947-952]. Furthermore, the histidine mutation significantly stabilized the open state, making the channels easier to open, slower to close, harder to inactivate and faster to recover from inactivation. Our finding that mutation of a single amino acid can greatly attenuate rundown provides an easy and efficient way to slow the rundown of VGCCs, facilitating functional studies that require direct access to the cytoplasmic side of the channel. Author Affiliation: Department of Biological Sciences, 917 Fairchild Center, MC2462, Columbia University, New York, NY 10027, USA Article History: Received 31 July 2006; Revised 6 September 2006; Accepted 13 September 2006
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