Journal
NATURE COMMUNICATIONS
Volume 11, Issue 1, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-020-16842-0
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Funding
- NHMRC Australia [1006624, 1080682]
- NHMRC Senior Research Fellowship
- Walter and Eliza Hall Institute
- Australian Postgraduate Award
- Australian Research Training Scholarships
- Medical Research Council [MR/N020413/1]
- Australian Government
- Intersect Australia Ltd
- LIEF Grant [LE170100200]
- MRC [MR/N020413/1] Funding Source: UKRI
- National Health and Medical Research Council of Australia [1080682] Funding Source: NHMRC
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The canonical mechanistic model explaining potassium channel gating is of a conformational change that alternately dilates and constricts a collar-like intracellular entrance to the pore. It is based on the premise that K+ ions maintain a complete hydration shell while passing between the transmembrane cavity and cytosol, which must be accommodated. To put the canonical model to the test, we locked the conformation of a Kir K+ channel to prevent widening of the narrow collar. Unexpectedly, conduction was unimpaired in the locked channels. In parallel, we employed all-atom molecular dynamics to simulate K+ ions moving along the conduction pathway between the lower cavity and cytosol. During simulations, the constriction did not significantly widen. Instead, transient loss of some water molecules facilitated K+ permeation through the collar. The low free energy barrier to partial dehydration in the absence of conformational change indicates Kir channels are not gated by the canonical mechanism.
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