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Title | Cryo-EM structure of the Slo1 potassium channel with the auxiliary γ1 subunit suggests a mechanism for depolarization-independent activation. |
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Journal, issue, pages | FEBS Lett, Vol. 598, Issue 8, Page 875-888, Year 2024 |
Publish date | Mar 30, 2024 |
Authors | Milena Redhardt / Stefan Raunser / Tobias Raisch / |
PubMed Abstract | Mammalian Ca-dependent Slo K channels can stably associate with auxiliary γ subunits which fundamentally alter their behavior. By a so far unknown mechanism, the four γ subunits reduce the need for ...Mammalian Ca-dependent Slo K channels can stably associate with auxiliary γ subunits which fundamentally alter their behavior. By a so far unknown mechanism, the four γ subunits reduce the need for voltage-dependent activation and, thereby, allow Slo to open independently of an action potential. Here, using cryo-EM, we reveal how the transmembrane helix of γ1/LRRC26 binds and presumably stabilizes the activated voltage-sensor domain of Slo1. The activation is further enhanced by an intracellular polybasic stretch which locally changes the charge gradient across the membrane. Our data provide a possible explanation for Slo1 regulation by the four γ subunits and also their different activation efficiencies. This suggests a novel activation mechanism of voltage-gated ion channels by auxiliary subunits. |
External links | FEBS Lett / PubMed:38553946 |
Methods | EM (single particle) |
Resolution | 2.39 Å |
Structure data | EMDB-19691, PDB-8s3e: |
Chemicals | ChemComp-CLR: ChemComp-CA: ChemComp-6PL: ChemComp-MG: ChemComp-K: ChemComp-HOH: |
Source |
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Keywords | MEMBRANE PROTEIN / Ion channel / potassium transport |