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TitleCryo-EM analysis of PIP regulation in mammalian GIRK channels.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateAug 26, 2020
AuthorsYiming Niu / Xiao Tao / Kouki K Touhara / Roderick MacKinnon /
PubMed AbstractG-protein-gated inward rectifier potassium (GIRK) channels are regulated by G proteins and PIP. Here, using cryo-EM single particle analysis we describe the equilibrium ensemble of structures of ...G-protein-gated inward rectifier potassium (GIRK) channels are regulated by G proteins and PIP. Here, using cryo-EM single particle analysis we describe the equilibrium ensemble of structures of neuronal GIRK2 as a function of the C8-PIP concentration. We find that PIP shifts the equilibrium between two distinguishable structures of neuronal GIRK (GIRK2), extended and docked, towards the docked form. In the docked form the cytoplasmic domain, to which G binds, becomes accessible to the cytoplasmic membrane surface where G resides. Furthermore, PIP binding reshapes the G binding surface on the cytoplasmic domain, preparing it to receive G. We find that cardiac GIRK (GIRK1/4) can also exist in both extended and docked conformations. These findings lead us to conclude that PIP influences GIRK channels in a structurally similar manner to Kir2.2 channels. In Kir2.2 channels, the PIP-induced conformational changes open the pore. In GIRK channels, they prepare the channel for activation by G.
External linksElife / PubMed:32844743 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 7.9 Å
Structure data

22199

6xis

EMDB-22199, PDB-6xis:
Cryo-EM structure of the G protein-gated inward rectifier K+ channel GIRK2 (Kir3.2) in apo form
Method: EM (single particle) / Resolution: 3.9 Å

22200

6xit

EMDB-22200, PDB-6xit:
Cryo-EM structure of the G protein-gated inward rectifier K+ channel GIRK2 (Kir3.2) in complex with PIP2
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-22201:
Cryo-EM structure of the G protein-gated inward rectifier K+ channel GIRK1/4 (Kir3.1/Kir3.4) in apo form
Method: EM (single particle) / Resolution: 7.9 Å

EMDB-22202:
Cryo-EM structure of the G protein-gated inward rectifier K+ channel GIRK1/4 (Kir3.1/Kir3.4) in complex with bound PIP2
Method: EM (single particle) / Resolution: 4.6 Å

Chemicals

ChemComp-PIO:
[(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate

ChemComp-K:
Unknown entry

Source
  • mus musculus (house mouse)
  • Homo sapiens (human)
KeywordsMEMBRANE PROTEIN / G protein-coupled inwardly rectifying potassium channels / PIP2

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