The isolated voltage sensing domain of the Shaker potassium channel forms a voltage-gated cation channel
Domains in macromolecular complexes are often considered structurally and functionally conserved while energetically coupled to each other. In the modular voltage-gated ion channels the central ion-conducting pore is surrounded by four voltage sensing domains (VSDs). Here, the energetic coupling is...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2016-10-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/18130 |
| _version_ | 1828166267679277056 |
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| author | Juan Zhao Rikard Blunck |
| author_facet | Juan Zhao Rikard Blunck |
| author_sort | Juan Zhao |
| collection | DOAJ |
| description | Domains in macromolecular complexes are often considered structurally and functionally conserved while energetically coupled to each other. In the modular voltage-gated ion channels the central ion-conducting pore is surrounded by four voltage sensing domains (VSDs). Here, the energetic coupling is mediated by interactions between the S4-S5 linker, covalently linking the domains, and the proximal C-terminus. In order to characterize the intrinsic gating of the voltage sensing domain in the absence of the pore domain, the Shaker Kv channel was truncated after the fourth transmembrane helix S4 (Shaker-iVSD). Shaker-iVSD showed significantly altered gating kinetics and formed a cation-selective ion channel with a strong preference for protons. Ion conduction in Shaker-iVSD developed despite identical primary sequence, indicating an allosteric influence of the pore domain. Shaker-iVSD also displays pronounced 'relaxation'. Closing of the pore correlates with entry into relaxation suggesting that the two processes are energetically related. |
| first_indexed | 2024-04-12T01:58:55Z |
| format | Article |
| id | doaj.art-347daba172fd4b8c823d33463c8e7b81 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T01:58:55Z |
| publishDate | 2016-10-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-347daba172fd4b8c823d33463c8e7b812022-12-22T03:52:43ZengeLife Sciences Publications LtdeLife2050-084X2016-10-01510.7554/eLife.18130The isolated voltage sensing domain of the Shaker potassium channel forms a voltage-gated cation channelJuan Zhao0Rikard Blunck1https://orcid.org/0000-0003-4484-2907Department of Physics, Université de Montréal, Montréal, Canada; Department of Pharmacology and Physiology, Université de Montréal, Montréal, CanadaDepartment of Physics, Université de Montréal, Montréal, Canada; Department of Pharmacology and Physiology, Université de Montréal, Montréal, CanadaDomains in macromolecular complexes are often considered structurally and functionally conserved while energetically coupled to each other. In the modular voltage-gated ion channels the central ion-conducting pore is surrounded by four voltage sensing domains (VSDs). Here, the energetic coupling is mediated by interactions between the S4-S5 linker, covalently linking the domains, and the proximal C-terminus. In order to characterize the intrinsic gating of the voltage sensing domain in the absence of the pore domain, the Shaker Kv channel was truncated after the fourth transmembrane helix S4 (Shaker-iVSD). Shaker-iVSD showed significantly altered gating kinetics and formed a cation-selective ion channel with a strong preference for protons. Ion conduction in Shaker-iVSD developed despite identical primary sequence, indicating an allosteric influence of the pore domain. Shaker-iVSD also displays pronounced 'relaxation'. Closing of the pore correlates with entry into relaxation suggesting that the two processes are energetically related.https://elifesciences.org/articles/18130voltage sensorpotassium channelgatingvoltage-clamp fluorometrymode-shift |
| spellingShingle | Juan Zhao Rikard Blunck The isolated voltage sensing domain of the Shaker potassium channel forms a voltage-gated cation channel eLife voltage sensor potassium channel gating voltage-clamp fluorometry mode-shift |
| title | The isolated voltage sensing domain of the Shaker potassium channel forms a voltage-gated cation channel |
| title_full | The isolated voltage sensing domain of the Shaker potassium channel forms a voltage-gated cation channel |
| title_fullStr | The isolated voltage sensing domain of the Shaker potassium channel forms a voltage-gated cation channel |
| title_full_unstemmed | The isolated voltage sensing domain of the Shaker potassium channel forms a voltage-gated cation channel |
| title_short | The isolated voltage sensing domain of the Shaker potassium channel forms a voltage-gated cation channel |
| title_sort | isolated voltage sensing domain of the shaker potassium channel forms a voltage gated cation channel |
| topic | voltage sensor potassium channel gating voltage-clamp fluorometry mode-shift |
| url | https://elifesciences.org/articles/18130 |
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