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TitleNoncanonical agonist-dependent and -independent arrestin recruitment of GPR1.
Journal, issue, pagesScience, Vol. 390, Issue 6775, Page eadt8794, Year 2025
Publish dateNov 20, 2025
AuthorsHeng Cai / Xiaowen Lin / Lechen Zhao / Maozhou He / Jie Yu / Bingjie Zhang / Yuandi Ma / Xiaohua Chang / Yuxuan Tang / Tianyu Luo / Jie Jiang / Mengna Ma / Wenqi Song / Limin Ma / Xiaojing Chu / Cuiying Yi / Kun Chen / Shuo Han / Cen Xie / Wenqing Shui / Qiang Zhao / Ya Zhu / Beili Wu /
PubMed AbstractG protein (heterotrimeric guanine nucleotide-binding protein)-coupled receptors have diverse signaling properties with differential preferences for downstream pathways. Certain receptors, such as the ...G protein (heterotrimeric guanine nucleotide-binding protein)-coupled receptors have diverse signaling properties with differential preferences for downstream pathways. Certain receptors, such as the chemerin receptor GPR1, undergo arrestin-mediated internalization but weak G protein signaling. However, the mechanisms of this unusual signaling pattern and its physiological relevance are unclear. We report the structures of GPR1 bound to chemerin and β-arrestin 1 or β-arrestin 2 and an agonist-free GPR1-β-arrestin 1 complex. Upon agonist stimulation, the receptor binds the two arrestins in distinct interaction patterns, which may account for their differential cellular responses. Agonist-independent internalization was mediated by an inactive, constitutively phosphorylated GPR1 that accommodates β-arrestin 1 in an unconventional pocket together with a fatty acid, which potentially provides a basis for GPR1 modulating lipid accumulation in lipid-overloaded adipocytes.
External linksScience / PubMed:41264711
MethodsEM (single particle)
Resolution2.9 - 3.5 Å
Structure data

64610

9uyh

EMDB-64610, PDB-9uyh:
Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 1 (Conformation 1)
Method: EM (single particle) / Resolution: 3.3 Å

64611

9uyi

EMDB-64611, PDB-9uyi:
Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 1 (Conformation 2)
Method: EM (single particle) / Resolution: 3.2 Å

64612

9uyj

EMDB-64612, PDB-9uyj:
Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 1 (Conformation 3)
Method: EM (single particle) / Resolution: 3.3 Å

64614

9uyl

EMDB-64614, PDB-9uyl:
Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 1 (Conformation 4)
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-64615: Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 2 (focused refinement in chemerin and GPR1)
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-64616: Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 2 (focused refinement in beta-arrestin 2)
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-64617: Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 2 (consensus refinement)
Method: EM (single particle) / Resolution: 3.4 Å

64618

9uym

EMDB-64618, PDB-9uym:
Composite map of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 2
Method: EM (single particle) / Resolution: 3.5 Å

64619

9uyn

EMDB-64619, PDB-9uyn:
Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to beta-arrestin 1 in ligand-free state
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-PAM:
PALMITOLEIC ACID

Source
  • homo sapiens (human)
  • escherichia phage ecszw-2 (virus)
KeywordsMEMBRANE PROTEIN/IMMUNE SYSTEM / G protein-coupled receptor 1 / chemerin / beta-arrestin1 / signaling protein / MEMBRANE PROTEIN-IMMUNE SYSTEM complex / beta-arrestin 2

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