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TitleCryo-EM structure of the Slo1 potassium channel with the auxiliary γ1 subunit suggests a mechanism for depolarization-independent activation.
Journal, issue, pagesFEBS Lett, Vol. 598, Issue 8, Page 875-888, Year 2024
Publish dateMar 30, 2024
AuthorsMilena Redhardt / Stefan Raunser / Tobias Raisch /
PubMed AbstractMammalian 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 linksFEBS Lett / PubMed:38553946
MethodsEM (single particle)
Resolution2.39 Å
Structure data

19691

8s3e

EMDB-19691, PDB-8s3e:
Structure of rabbit Slo1 in complex with gamma1/LRRC26
Method: EM (single particle) / Resolution: 2.39 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL / Cholesterol

ChemComp-CA:
Unknown entry

ChemComp-6PL:
(4S,7R)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE / phospholipid*YM

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • oryctolagus cuniculus (rabbit)
KeywordsMEMBRANE PROTEIN / Ion channel / potassium transport

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