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Structure paper

TitleMembrane phospholipids control gating of the mechanosensitive potassium leak channel TREK1.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 1077, Year 2023
Publish dateFeb 25, 2023
AuthorsPhilipp A M Schmidpeter / John T Petroff / Leila Khajoueinejad / Aboubacar Wague / Cheryl Frankfater / Wayland W L Cheng / Crina M Nimigean / Paul M Riegelhaupt /
PubMed AbstractTandem pore domain (K2P) potassium channels modulate resting membrane potentials and shape cellular excitability. For the mechanosensitive subfamily of K2Ps, the composition of phospholipids within ...Tandem pore domain (K2P) potassium channels modulate resting membrane potentials and shape cellular excitability. For the mechanosensitive subfamily of K2Ps, the composition of phospholipids within the bilayer strongly influences channel activity. To examine the molecular details of K2P lipid modulation, we solved cryo-EM structures of the TREK1 K2P channel bound to either the anionic lipid phosphatidic acid (PA) or the zwitterionic lipid phosphatidylethanolamine (PE). At the extracellular face of TREK1, a PA lipid inserts its hydrocarbon tail into a pocket behind the selectivity filter, causing a structural rearrangement that recapitulates mutations and pharmacology known to activate TREK1. At the cytoplasmic face, PA and PE lipids compete to modulate the conformation of the TREK1 TM4 gating helix. Our findings demonstrate two distinct pathways by which anionic lipids enhance TREK1 activity and provide a framework for a model that integrates lipid gating with the effects of other mechanosensitive K2P modulators.
External linksNat Commun / PubMed:36841877 / PubMed Central
MethodsEM (single particle)
Resolution2.82 - 3.4 Å
Structure data

27386

8de7

EMDB-27386, PDB-8de7:
Cryo-EM structure of the zebrafish two pore domain K+ channel TREK1 (K2P2.1) in DDM detergent
Method: EM (single particle) / Resolution: 3.27 Å

27387

8de8

EMDB-27387, PDB-8de8:
Cryo-EM structure of the zebrafish two pore domain K+ channel TREK1 (K2P2.1) in DDM/POPA mixed micelles
Method: EM (single particle) / Resolution: 2.82 Å

27388

8de9

EMDB-27388, PDB-8de9:
Cryo-EM structure of the zebrafish two pore domain K+ channel TREK1 (K2P2.1) in DDM/POPE mixed micelles
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-K:
Unknown entry

ChemComp-D21:
(2R)-1-(hexadecanoyloxy)-3-(phosphonooxy)propan-2-yl (9Z)-octadec-9-enoate

ChemComp-PEV:
(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / POPE, phospholipid*YM / Phosphatidylethanolamine

Source
  • danio rerio (zebrafish)
KeywordsMEMBRANE PROTEIN / ion channel / K2P / K2P2.1 / TREK1 / TREK-1 / phospholipid / POPA / POPE

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