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Structure paper

TitleMolecular architecture of the Gα-bound TRPC5 ion channel.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 2550, Year 2023
Publish dateMay 3, 2023
AuthorsJongdae Won / Jinsung Kim / Hyeongseop Jeong / Jinhyeong Kim / Shasha Feng / Byeongseok Jeong / Misun Kwak / Juyeon Ko / Wonpil Im / Insuk So / Hyung Ho Lee /
PubMed AbstractG-protein coupled receptors (GPCRs) and ion channels serve as key molecular switches through which extracellular stimuli are transformed into intracellular effects, and it has long been postulated ...G-protein coupled receptors (GPCRs) and ion channels serve as key molecular switches through which extracellular stimuli are transformed into intracellular effects, and it has long been postulated that ion channels are direct effector molecules of the alpha subunit of G-proteins (Gα). However, no complete structural evidence supporting the direct interaction between Gα and ion channels is available. Here, we present the cryo-electron microscopy structures of the human transient receptor potential canonical 5 (TRPC5)-Gα complexes with a 4:4 stoichiometry in lipid nanodiscs. Remarkably, Gα binds to the ankyrin repeat edge of TRPC5 ~ 50 Å away from the cell membrane. Electrophysiological analysis shows that Gα increases the sensitivity of TRPC5 to phosphatidylinositol 4,5-bisphosphate (PIP), thereby rendering TRPC5 more easily opened in the cell membrane, where the concentration of PIP is physiologically regulated. Our results demonstrate that ion channels are one of the direct effector molecules of Gα proteins triggered by GPCR activation-providing a structural framework for unraveling the crosstalk between two major classes of transmembrane proteins: GPCRs and ion channels.
External linksNat Commun / PubMed:37137991 / PubMed Central
MethodsEM (single particle)
Resolution3.15 - 3.93 Å
Structure data

33021

7x6c

EMDB-33021, PDB-7x6c:
Cryo-EM structure of the human TRPC5 ion channel in lipid nanodiscs, class1
Method: EM (single particle) / Resolution: 3.15 Å

33022

7x6i

EMDB-33022, PDB-7x6i:
Cryo-EM structure of the human TRPC5 ion channel in complex with G alpha i3 subunits, class1
Method: EM (single particle) / Resolution: 3.93 Å

34300

8gvw

EMDB-34300, PDB-8gvw:
Cryo-EM structure of the human TRPC5 ion channel in lipid nanodiscs, class2
Method: EM (single particle) / Resolution: 3.59 Å

34301

8gvx

EMDB-34301, PDB-8gvx:
Cryo-EM structure of the human TRPC5 ion channel in complex with G alpha i3 subunits, class2
Method: EM (single particle) / Resolution: 3.91 Å

Chemicals

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM / Phosphatidylethanolamine

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM / POPC

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-ZN:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-YZY:
(2S)-2-(hexadecanoyloxy)-3-hydroxypropyl (9Z)-octadec-9-enoate

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

Source
  • homo sapiens (human)
KeywordsMETAL TRANSPORT / TRP / transient receptor potential

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