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Structure paper

TitleStructural characterization of five functional states of metabotropic glutamate receptor 8.
Journal, issue, pagesMol Cell, Vol. 85, Issue 18, Page 3460-33473.e6, Year 2025
Publish dateSep 18, 2025
AuthorsJie Zhao / Yue Deng / Zheng Xu / Chanjuan Xu / Chang Zhao / Ziyan Li / Hui Sun / Xiaowen Tian / Yuxuan Song / Marta Cimadevila / Heli Wang / Yuxuan Liu / Xiaoyu Zhang / Yiyang Chen / Suyue Sun / Xihao Yong / Lantian Su / Yixiao He / Yi Zhong / Hao Yang / Jean-Philippe Pin / Wei Yan / Zhenhua Shao / Jianfeng Liu /
PubMed AbstractMetabotropic glutamate receptors (mGluRs) are dimeric class C G protein-coupled receptors, which play crucial roles in brain physiology and pathology. Among them, mGlu8 is the least characterized, ...Metabotropic glutamate receptors (mGluRs) are dimeric class C G protein-coupled receptors, which play crucial roles in brain physiology and pathology. Among them, mGlu8 is the least characterized, though it is physiologically important. While recognized to signal via G proteins, the involvement of β-arrestin is unknown. Here, we found that both mGlu8 agonists and positive allosteric modulators (PAMs) activate G signaling, but mainly agonists induce β-arrestin recruitment. We solved five human mGlu8 cryo-electron microscopy (cryo-EM) structures in various states: apo, antagonist-bound, agonist + PAM-bound, agonist + PAM-bound with G protein, and agonist-bound with β-arrestin1 states. They revealed a unique PAM-binding pocket at the extracellular side of the TM6/TM7 interface. Agonist and PAM promote active mGlu8 association with one G protein asymmetrically (2:1), while two β-arrestin1 can interact symmetrically (2:2) to both subunits of an inactive dimer state to promote constitutive internalization. These findings elucidate how mGlu8 selectively engages transducers, offering insights into its signaling capabilities and selective drug development.
External linksMol Cell / PubMed:40972528
MethodsEM (single particle)
Resolution2.97 - 3.32 Å
Structure data

63770

9mb9

EMDB-63770, PDB-9mb9:
Cryo-EM structure of Gi-bound GPCR
Method: EM (single particle) / Resolution: 2.97 Å

63771

9mba

EMDB-63771, PDB-9mba:
Cryo-EM structure of complex of transducer-bound GPCR
Method: EM (single particle) / Resolution: 3.14 Å

63772

9mbb

EMDB-63772, PDB-9mbb:
Cryo-EM structure of antagonist-bound GPCR
Method: EM (single particle) / Resolution: 3.25 Å

63773

9mbc

EMDB-63773, PDB-9mbc:
Cryo-EM structure of agonist-bound GPCR
Method: EM (single particle) / Resolution: 2.97 Å

63774

9mbd

EMDB-63774, PDB-9mbd:
Cryo-EM structure of Apo-GPCR
Method: EM (single particle) / Resolution: 3.32 Å

Chemicals

ChemComp-HVG:
4-[(S)-amino(carboxy)methyl]benzene-1,2-dicarboxylic acid / agonist*YM

PDB-1ens:
CRYSTALS OF DEMETALLIZED CONCANAVALIN A SOAKED WITH COBALT HAVING A COBALT ION BOUND IN THE S1 SITE

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-Z99:
2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine / antidepressant, antagonist*YM

PDB-1enr:
CO-CRYSTALS OF DEMETALLIZED CONCANAVALIN A WITH ZINC AND CALCIUM HAVING A ZINC ION BOUND IN THE S1 SITE AND A CALCIUM ION BOUND IN THE S2 SITE

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / Complex / PROTEIN / Antagonist / MEMBRANE / MEMBRANE PROTEIN-IMMUNE SYSTEM complex / Arrestin / Singaling protein / Agonist / PAM

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