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Structure paper

TitleMolecular basis of β-arrestin coupling to the metabotropic glutamate receptor mGlu3.
Journal, issue, pagesNat Chem Biol, Vol. 21, Issue 8, Page 1262-1269, Year 2025
Publish dateMar 6, 2025
AuthorsTianlei Wen / Mei Du / Yue Lu / Nan Jia / Xuhang Lu / Ning Liu / Shenghai Chang / Xing Zhang / Yuequan Shen / Xue Yang /
PubMed Abstractβ-Arrestins (βarrs) mediate the desensitization and internalization of activated G-protein-coupled receptors (GPCRs). The molecular mechanism by which dimeric family C GPCR members recruit ...β-Arrestins (βarrs) mediate the desensitization and internalization of activated G-protein-coupled receptors (GPCRs). The molecular mechanism by which dimeric family C GPCR members recruit arrestins remains elusive. Here we report two structures of metabotropic glutamate receptor subtype 3 (mGlu3) coupled to βarr1, with stoichiometries of 2:1 and 2:2. The L-glutamate-bound mGlu3 dimer adopts an inactive state, with both Venus flytrap domains closed, engaging βarr1 either asymmetrically or symmetrically. The transmembrane domain of the mGlu3 protomer interacts with βarr1 through a binding pocket formed by three intracellular loops and an ordered C-terminal region. Three phosphorylation sites (pS857, pS859 and pT860) on the C-terminal tail of mGlu3 engage the N domain of βarr1. βarr1 stabilizes mGlu3 in an inactive conformation, characterized by a TM3/TM4-TM3/TM4 dimeric interface, previously observed in the negative allosteric modulator-bound structure of mGlu3. Our findings provide important insights into βarr-mediated inactivation of family C GPCRs.
External linksNat Chem Biol / PubMed:40050438
MethodsEM (single particle)
Resolution3.6 - 3.9 Å
Structure data

60588

9ii2

EMDB-60588, PDB-9ii2:
Cryo-EM Structure of the 2:2 Complex of mGlu3 and beta-arrestin1
Method: EM (single particle) / Resolution: 3.7 Å

60589

9ii3

EMDB-60589, PDB-9ii3:
Cryo-EM Structure of the 2:1 Complex of mGlu3 and beta-arrestin1
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-60942: Focused map of mGlu3 and beta-arrestin1 2:2 Compex ECD domain (PDB 9II2)
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / complex

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