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Structure paper

TitleConstitutive activation mechanism of a class C GPCR.
Journal, issue, pagesNat Struct Mol Biol, Vol. 31, Issue 4, Page 678-687, Year 2024
Publish dateFeb 8, 2024
AuthorsJinwoo Shin / Junhyeon Park / Jieun Jeong / Jordy Homing Lam / Xingyu Qiu / Di Wu / Kuglae Kim / Joo-Youn Lee / Carol V Robinson / Jaekyung Hyun / Vsevolod Katritch / Kwang Pyo Kim / Yunje Cho /
PubMed AbstractClass C G-protein-coupled receptors (GPCRs) are activated through binding of agonists to the large extracellular domain (ECD) followed by rearrangement of the transmembrane domains (TMDs). GPR156, a ...Class C G-protein-coupled receptors (GPCRs) are activated through binding of agonists to the large extracellular domain (ECD) followed by rearrangement of the transmembrane domains (TMDs). GPR156, a class C orphan GPCR, is unique because it lacks an ECD and exhibits constitutive activity. Impaired GPR156-G signaling contributes to loss of hearing. Here we present the cryo-electron microscopy structures of human GPR156 in the G-free and G-coupled states. We found that an endogenous phospholipid molecule is located within each TMD of the GPR156 dimer. Asymmetric binding of Gα to the phospholipid-bound GPR156 dimer restructures the first and second intracellular loops and the carboxy-terminal part of the elongated transmembrane 7 (TM7) without altering dimer conformation. Our findings reveal that GPR156 is a transducer for phospholipid signaling. Constant binding of abundant phospholipid molecules and the G-protein-induced reshaping of the cytoplasmic face provide a basis for the constitutive activation of GPR156.
External linksNat Struct Mol Biol / PubMed:38332368
MethodsEM (single particle)
Resolution2.61 - 3.33 Å
Structure data

35377

8ieb

EMDB-35377, PDB-8ieb:
Cryo-EM structure of GPR156 of GPR156-miniGo-scFv16 complex (local refine)
Method: EM (single particle) / Resolution: 3.03 Å

35378

8iec

EMDB-35378, PDB-8iec:
Cryo-EM structure of miniGo-scFv16 of GPR156-miniGo-scFv16 complex (local refine)
Method: EM (single particle) / Resolution: 3.18 Å

35380

8ied

EMDB-35380, PDB-8ied:
Cryo-EM structure of GPR156-miniGo-scFv16 complex
Method: EM (single particle) / Resolution: 3.33 Å

35382

8iei

EMDB-35382, PDB-8iei:
Cryo-EM structure of GPR156A/B of G-protein free GPR156 (local refine)
Method: EM (single particle) / Resolution: 2.62 Å

35389

8iep

EMDB-35389, PDB-8iep:
Cryo-EM structure of GPR156C/D of G-protein free GPR156 (local refine)
Method: EM (single particle) / Resolution: 2.61 Å

35390

8ieq

EMDB-35390, PDB-8ieq:
Cryo-EM structure of G-protein free GPR156
Method: EM (single particle) / Resolution: 2.73 Å

Chemicals

PDB-1lya:
CRYSTAL STRUCTURES OF NATIVE AND INHIBITED FORMS OF HUMAN CATHEPSIN D: IMPLICATIONS FOR LYSOSOMAL TARGETING AND DRUG DESIGN

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsSIGNALING PROTEIN / Membrane protein / G-protein coupled receptor / Signal transduction / Phospholipid

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