The Voltage-Dependent Deactivation of the KvAP Channel Involves the Breakage of Its S4 Helix Article Swipe
Olivier Bignucolo
,
Simon Bernèche
·
YOU?
·
· 2020
· Open Access
·
· DOI: https://doi.org/10.3389/fmolb.2020.00162
YOU?
·
· 2020
· Open Access
·
· DOI: https://doi.org/10.3389/fmolb.2020.00162
Voltage-gated potassium channels (Kv) allow ion permeation upon changes of the membrane electrostatic potential (Vm). Each subunit of these tetrameric channels is composed of six transmembrane helices, of which the anti-parallel helix bundle S1-S4 constitutes the voltage-sensor domain (VSD) and S5-S6 forms the pore domain. Here, using 82 molecular dynamics (MD) simulations involving 266 replicated VSDs, we report novel responses of the archaebacterial potassium channel KvAP to membrane polarization. We show that the S4 α-helix, which is straight in the experimental crystal structure solved under depolarized conditions (Vm ∼ 0), breaks into two segments when the cell membrane is hyperpolarized (Vm << 0), and reversibly forms a single straight helix following depolarization (Vm = 0). The outermost segment of S4 translates along the normal to the membrane, bringing new perspective to previously paradoxical accessibility experiments that were initially thought to imply the displacement of the whole VSD across the membrane. The novel model is applied through steered and unbiased MD simulations to the recently solved whole structure of KvAP. The simulations show that the resting state involves a re-orientation of the S5 α-helix by ∼ 5-6 degrees in respect to the normal of the bilayer, which could result in the constriction and closure of the selectivity filter. Our findings support the idea that the breakage of S4 under (hyper)polarization is a general feature of Kv channels with a non-swapped topology.
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Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.3389/fmolb.2020.00162
- https://www.frontiersin.org/articles/10.3389/fmolb.2020.00162/pdf
- OA Status
- gold
- Cited By
- 9
- References
- 75
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W3046167158
All OpenAlex metadata
Raw OpenAlex JSON
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https://openalex.org/W3046167158Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.3389/fmolb.2020.00162Digital Object Identifier
- Title
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The Voltage-Dependent Deactivation of the KvAP Channel Involves the Breakage of Its S4 HelixWork title
- Type
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articleOpenAlex work type
- Language
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enPrimary language
- Publication year
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2020Year of publication
- Publication date
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2020-07-29Full publication date if available
- Authors
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Olivier Bignucolo, Simon BernècheList of authors in order
- Landing page
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https://doi.org/10.3389/fmolb.2020.00162Publisher landing page
- PDF URL
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https://www.frontiersin.org/articles/10.3389/fmolb.2020.00162/pdfDirect link to full text PDF
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YesWhether a free full text is available
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goldOpen access status per OpenAlex
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https://www.frontiersin.org/articles/10.3389/fmolb.2020.00162/pdfDirect OA link when available
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Helix (gastropod), Breakage, Chemistry, hERG, Biophysics, Potassium channel, Biology, Materials science, Ecology, Snail, Composite materialTop concepts (fields/topics) attached by OpenAlex
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9Total citation count in OpenAlex
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2025: 1, 2024: 3, 2023: 3, 2021: 2Per-year citation counts (last 5 years)
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75Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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