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S1 Constrains S4 in the Voltage Sensor Domain of Kv7.1 K(+) Channels
Voltage-gated K(+) channels comprise a central pore enclosed by four voltage-sensing domains (VSDs). While movement of the S4 helix is known to couple to channel gate opening and closing, the nature of S4 motion is unclear. Here, we substituted S4 residues of Kv7.1 channels by cysteine and recorded...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Public Library of Science
2008
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2275789/ https://www.ncbi.nlm.nih.gov/pubmed/18398461 http://dx.doi.org/10.1371/journal.pone.0001935 |
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author | Haitin, Yoni Yisharel, Ilanit Malka, Eti Shamgar, Liora Schottelndreier, Hella Peretz, Asher Paas, Yoav Attali, Bernard |
author_facet | Haitin, Yoni Yisharel, Ilanit Malka, Eti Shamgar, Liora Schottelndreier, Hella Peretz, Asher Paas, Yoav Attali, Bernard |
author_sort | Haitin, Yoni |
collection | PubMed |
description | Voltage-gated K(+) channels comprise a central pore enclosed by four voltage-sensing domains (VSDs). While movement of the S4 helix is known to couple to channel gate opening and closing, the nature of S4 motion is unclear. Here, we substituted S4 residues of Kv7.1 channels by cysteine and recorded whole-cell mutant channel currents in Xenopus oocytes using the two-electrode voltage-clamp technique. In the closed state, disulfide and metal bridges constrain residue S225 (S4) nearby C136 (S1) within the same VSD. In the open state, two neighboring I227 (S4) are constrained at proximity while residue R228 (S4) is confined close to C136 (S1) of an adjacent VSD. Structural modeling predicts that in the closed to open transition, an axial rotation (∼190°) and outward translation of S4 (∼12 Å) is accompanied by VSD rocking. This large sensor motion changes the intra-VSD S1–S4 interaction to an inter-VSD S1–S4 interaction. These constraints provide a ground for cooperative subunit interactions and suggest a key role of the S1 segment in steering S4 motion during Kv7.1 gating. |
format | Text |
id | pubmed-2275789 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-22757892008-04-09 S1 Constrains S4 in the Voltage Sensor Domain of Kv7.1 K(+) Channels Haitin, Yoni Yisharel, Ilanit Malka, Eti Shamgar, Liora Schottelndreier, Hella Peretz, Asher Paas, Yoav Attali, Bernard PLoS One Research Article Voltage-gated K(+) channels comprise a central pore enclosed by four voltage-sensing domains (VSDs). While movement of the S4 helix is known to couple to channel gate opening and closing, the nature of S4 motion is unclear. Here, we substituted S4 residues of Kv7.1 channels by cysteine and recorded whole-cell mutant channel currents in Xenopus oocytes using the two-electrode voltage-clamp technique. In the closed state, disulfide and metal bridges constrain residue S225 (S4) nearby C136 (S1) within the same VSD. In the open state, two neighboring I227 (S4) are constrained at proximity while residue R228 (S4) is confined close to C136 (S1) of an adjacent VSD. Structural modeling predicts that in the closed to open transition, an axial rotation (∼190°) and outward translation of S4 (∼12 Å) is accompanied by VSD rocking. This large sensor motion changes the intra-VSD S1–S4 interaction to an inter-VSD S1–S4 interaction. These constraints provide a ground for cooperative subunit interactions and suggest a key role of the S1 segment in steering S4 motion during Kv7.1 gating. Public Library of Science 2008-04-09 /pmc/articles/PMC2275789/ /pubmed/18398461 http://dx.doi.org/10.1371/journal.pone.0001935 Text en Haitin et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Haitin, Yoni Yisharel, Ilanit Malka, Eti Shamgar, Liora Schottelndreier, Hella Peretz, Asher Paas, Yoav Attali, Bernard S1 Constrains S4 in the Voltage Sensor Domain of Kv7.1 K(+) Channels |
title | S1 Constrains S4 in the Voltage Sensor Domain of Kv7.1 K(+) Channels |
title_full | S1 Constrains S4 in the Voltage Sensor Domain of Kv7.1 K(+) Channels |
title_fullStr | S1 Constrains S4 in the Voltage Sensor Domain of Kv7.1 K(+) Channels |
title_full_unstemmed | S1 Constrains S4 in the Voltage Sensor Domain of Kv7.1 K(+) Channels |
title_short | S1 Constrains S4 in the Voltage Sensor Domain of Kv7.1 K(+) Channels |
title_sort | s1 constrains s4 in the voltage sensor domain of kv7.1 k(+) channels |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2275789/ https://www.ncbi.nlm.nih.gov/pubmed/18398461 http://dx.doi.org/10.1371/journal.pone.0001935 |
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