A Common Structural Component for β-Subunit Mediated Modulation of Slow Inactivation in Different KV Channels

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A Common Structural Component for β-Subunit Mediated Modulation of Slow Inactivation in Different KV Channels. / Strutz-Seebohm, Nathalie; Henrion, Ulrike; Schmitt, Nicole; Schulze-Bahr, Eric; Seebohm, Guiscard.

In: Cellular Physiology and Biochemistry, Vol. 31, No. 6, 26.06.2013, p. 968-980.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Strutz-Seebohm, N, Henrion, U, Schmitt, N, Schulze-Bahr, E & Seebohm, G 2013, 'A Common Structural Component for β-Subunit Mediated Modulation of Slow Inactivation in Different KV Channels', Cellular Physiology and Biochemistry, vol. 31, no. 6, pp. 968-980. https://doi.org/10.1159/000350115

APA

Strutz-Seebohm, N., Henrion, U., Schmitt, N., Schulze-Bahr, E., & Seebohm, G. (2013). A Common Structural Component for β-Subunit Mediated Modulation of Slow Inactivation in Different KV Channels. Cellular Physiology and Biochemistry, 31(6), 968-980. https://doi.org/10.1159/000350115

Vancouver

Strutz-Seebohm N, Henrion U, Schmitt N, Schulze-Bahr E, Seebohm G. A Common Structural Component for β-Subunit Mediated Modulation of Slow Inactivation in Different KV Channels. Cellular Physiology and Biochemistry. 2013 Jun 26;31(6):968-980. https://doi.org/10.1159/000350115

Author

Strutz-Seebohm, Nathalie ; Henrion, Ulrike ; Schmitt, Nicole ; Schulze-Bahr, Eric ; Seebohm, Guiscard. / A Common Structural Component for β-Subunit Mediated Modulation of Slow Inactivation in Different KV Channels. In: Cellular Physiology and Biochemistry. 2013 ; Vol. 31, No. 6. pp. 968-980.

Bibtex

@article{1f3ddc009efd4fe89bd2852b3ac4d4ad,
title = "A Common Structural Component for β-Subunit Mediated Modulation of Slow Inactivation in Different KV Channels",
abstract = "Background/Aims: Potassium channels are tetrameric proteins providing potassium selective passage through lipid embedded proteinaceous pores with highest fidelity. The selectivity results from binding to discrete potassium binding sites and stabilization of a hydrated potassium ion in a central internal cavity. The four potassium binding sites, generated by the conserved TTxGYGD signature sequence are formed by the backbone carbonyls of the amino acids TXGYG. Residues KV1.5-Val481, KV4.3-Leu368 and KV7.1- Ile 313 represent the amino acids in the X position of the respective channels. Methods: Here, we study the impact of these residues on ion selectivity, permeation and inactivation kinetics as well as the modulation by β-subunits using site-specific mutagenesis, electrophysiological analyses and molecular dynamics simulations. Results: We identify this position as key in modulation of slow inactivation by structurally dissimilar β-subunits in different KV channels. Conclusion: We propose a model in which structural changes accompanying activation and β-subunit modulation allosterically constrain the backbone carbonyl oxygen atoms via the side chain of the respective X-residue in the signature sequence to reduce conductance during slow inactivation.",
author = "Nathalie Strutz-Seebohm and Ulrike Henrion and Nicole Schmitt and Eric Schulze-Bahr and Guiscard Seebohm",
note = "Copyright {\circledC} 2013 S. Karger AG, Basel.",
year = "2013",
month = "6",
day = "26",
doi = "10.1159/000350115",
language = "English",
volume = "31",
pages = "968--980",
journal = "Cellular Physiology and Biochemistry",
issn = "1015-8987",
publisher = "S Karger AG",
number = "6",

}

RIS

TY - JOUR

T1 - A Common Structural Component for β-Subunit Mediated Modulation of Slow Inactivation in Different KV Channels

AU - Strutz-Seebohm, Nathalie

AU - Henrion, Ulrike

AU - Schmitt, Nicole

AU - Schulze-Bahr, Eric

AU - Seebohm, Guiscard

N1 - Copyright © 2013 S. Karger AG, Basel.

PY - 2013/6/26

Y1 - 2013/6/26

N2 - Background/Aims: Potassium channels are tetrameric proteins providing potassium selective passage through lipid embedded proteinaceous pores with highest fidelity. The selectivity results from binding to discrete potassium binding sites and stabilization of a hydrated potassium ion in a central internal cavity. The four potassium binding sites, generated by the conserved TTxGYGD signature sequence are formed by the backbone carbonyls of the amino acids TXGYG. Residues KV1.5-Val481, KV4.3-Leu368 and KV7.1- Ile 313 represent the amino acids in the X position of the respective channels. Methods: Here, we study the impact of these residues on ion selectivity, permeation and inactivation kinetics as well as the modulation by β-subunits using site-specific mutagenesis, electrophysiological analyses and molecular dynamics simulations. Results: We identify this position as key in modulation of slow inactivation by structurally dissimilar β-subunits in different KV channels. Conclusion: We propose a model in which structural changes accompanying activation and β-subunit modulation allosterically constrain the backbone carbonyl oxygen atoms via the side chain of the respective X-residue in the signature sequence to reduce conductance during slow inactivation.

AB - Background/Aims: Potassium channels are tetrameric proteins providing potassium selective passage through lipid embedded proteinaceous pores with highest fidelity. The selectivity results from binding to discrete potassium binding sites and stabilization of a hydrated potassium ion in a central internal cavity. The four potassium binding sites, generated by the conserved TTxGYGD signature sequence are formed by the backbone carbonyls of the amino acids TXGYG. Residues KV1.5-Val481, KV4.3-Leu368 and KV7.1- Ile 313 represent the amino acids in the X position of the respective channels. Methods: Here, we study the impact of these residues on ion selectivity, permeation and inactivation kinetics as well as the modulation by β-subunits using site-specific mutagenesis, electrophysiological analyses and molecular dynamics simulations. Results: We identify this position as key in modulation of slow inactivation by structurally dissimilar β-subunits in different KV channels. Conclusion: We propose a model in which structural changes accompanying activation and β-subunit modulation allosterically constrain the backbone carbonyl oxygen atoms via the side chain of the respective X-residue in the signature sequence to reduce conductance during slow inactivation.

U2 - 10.1159/000350115

DO - 10.1159/000350115

M3 - Journal article

C2 - 23839156

VL - 31

SP - 968

EP - 980

JO - Cellular Physiology and Biochemistry

JF - Cellular Physiology and Biochemistry

SN - 1015-8987

IS - 6

ER -

ID: 47327687