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TitleMolecular insights into the activation mechanism of GPR156 in maintaining auditory function.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 10601, Year 2024
Publish dateDec 5, 2024
AuthorsXiangyu Ma / Li-Nan Chen / Menghui Liao / Liyan Zhang / Kun Xi / Jiamin Guo / Cangsong Shen / Dan-Dan Shen / Pengjun Cai / Qingya Shen / Jieyu Qi / Huibing Zhang / Shao-Kun Zang / Ying-Jun Dong / Luwei Miao / Jiao Qin / Su-Yu Ji / Yue Li / Jianfeng Liu / Chunyou Mao / Yan Zhang / Renjie Chai /
PubMed AbstractThe class C orphan G-protein-coupled receptor (GPCR) GPR156, which lacks the large extracellular region, plays a pivotal role in auditory function through G. Here, we firstly demonstrate that GPR156 ...The class C orphan G-protein-coupled receptor (GPCR) GPR156, which lacks the large extracellular region, plays a pivotal role in auditory function through G. Here, we firstly demonstrate that GPR156 with high constitutive activity is essential for maintaining auditory function, and further reveal the structural basis of the sustained role of GPR156. We present the cryo-EM structures of human apo GPR156 and the GPR156-G complex, unveiling a small extracellular region formed by extracellular loop 2 (ECL2) and the N-terminus. The GPR156 dimer in both apo state and G protein-coupled state adopt a transmembrane (TM)5/6-TM5/6 interface, indicating the high constitutive activity of GPR156 in the apo state. Furthermore, C-terminus in G-bound subunit of GPR156 plays a dual role in promoting G protein binding within G-bound subunit while preventing the G-free subunit from binding to additional G protein. Together, these results explain how GPR156 constitutive activity is maintained through dimerization and provide a mechanistic insight into the sustained role of GPR156 in maintaining auditory function.
External linksNat Commun / PubMed:39638804 / PubMed Central
MethodsEM (single particle)
Resolution2.4 - 3.09 Å
Structure data

39345

8yjp

EMDB-39345, PDB-8yjp:
Cryo-EM structure of human apo GPR156
Method: EM (single particle) / Resolution: 3.09 Å

39356

8yk0

EMDB-39356, PDB-8yk0:
Cryo-EM structure of human GPR156-Gi3 complex
Method: EM (single particle) / Resolution: 2.4 Å

Chemicals

ChemComp-MW9:
(21R,24R,27S)-24,27,28-trihydroxy-18,24-dioxo-19,23,25-trioxa-24lambda~5~-phosphaoctacosan-21-yl (9Z)-octadec-9-enoate

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
  • rattus norvegicus (Norway rat)
  • bos taurus (cattle)
KeywordsMEMBRANE PROTEIN / GPCR / class C / GPR156 / cryo-EM / homodimer / active state

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