This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 12 digital issues and online access to articles
$119.00 per year
only $9.92 per issue
Buy this article
- Purchase on SpringerLink
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Data availability
Cryo-EM maps and structure coordinates have been deposited in the Electron Microscopy Data Bank (EMDB) and Protein Data Bank (PDB) with accession codes EMD-60643 and 9IJS for the apo GPR52–βarr1–scFv30 complex; EMD-60642 and 9IJR for the c17–GPR52–βarr1–scFv30 complex.
References
Liao, Y. Y. et al. Cell 186, 5784–5797.e17 (2023).
Chen, K. et al. Nature 620, 904–910 (2023).
Staus, D. P. et al. Nature 579, 297–302 (2020).
Ali, S. et al. Drug Discov. Today 29, 103922 (2024).
Yao, Y. et al. Elife 4, e05449 (2015).
Wang, C. et al. J. Med. Chem. 64, 941–957 (2021).
Martin, A. L. et al. PLoS One 10, e0138463 (2015).
Lin, X. et al. Nature 579, 152–157 (2020).
Lin, X. et al. Cell Discov. 9, 23 (2023).
Hoppe, N. et al. Nat. Struct. Mol. Biol. 31, 667–677 (2024).
Li, F. et al. Cell Commun. Signal. 17, 49 (2019).
Wang, W. W. et al. Cell 187, 1460–1475.e20 (2024).
Yue, Y. et al. Nat. Struct. Mol. Biol. 29, 688–697 (2022).
Lin, X. et al. Nat. Commun. 14, 216 (2023).
Yin, W. et al. Cell Res. 29, 971–983 (2019).
Sun, D. et al. Cell Res. 35, 284–295 (2025).
Acknowledgements
This work was supported by the National Natural Science Foundation of China (W2412030 to F.X.), Shanghai DFYC Program (to F.X.), Shanghai Chenguang Program (23CGA79 to X.L.), and Innovative research team of high-level local universities in Shanghai. The cryo-EM data were collected at the Bio-EM Facility, ShanghaiTech University, with the assistance of Li Wang, Dandan Liu, and Yuan Pei, and other staff members. We thank Bingjie Zhang and Wenqing Shui for insightful discussions on phosphorylation. We also thank the staff members of the Cell Expression, Assay, Cloning, and Purification Core Facilities of iHuman Institute for their support.
Author information
Authors and Affiliations
Contributions
X.L. performed cryo-EM sample preparation, data collection, structure determination and HTRF assay. X.W. conducted the piggyBac-based TANGO GFP assay and imaging. N.P. conducted the relevant work on the truncated complex. L.W. performed arrestin recruitment assay. Z.Z. assisted with EM data processing. C.L. synthesized the GPR52 agonist. Y.Y. assisted with APJR-related assays. J.L. performed protein expression. Q.T. assisted with the arrestin recruitment assay. Q.S. assisted with EM data collection. F.X. conceived the project, designed and supervised experiments. X.L. and F.X. wrote the manuscript with the input from all authors.
Corresponding authors
Ethics declarations
Competing interests
The authors declare no competing interests.
Additional information
Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Supplementary information
Rights and permissions
About this article
Cite this article
Lin, X., Wei, X., Pu, N. et al. Constitutive arrestin recruitment by orphan GPR52 via an atypical binding mode. Cell Res (2025). https://doi.org/10.1038/s41422-025-01165-w
Received:
Accepted:
Published:
DOI: https://doi.org/10.1038/s41422-025-01165-w
