Cryo-EM structure of cannabinoid receptor CB1-β-arrestin complex

doi:10.1093/procel/pwad055

Protein Cell

2024, Vol. 15

Issue (3) : 230-234 https://doi.org/10.1093/procel/pwad055

Cryo-EM structure of cannabinoid receptor CB1-β-arrestin complex

Yuxia Wang¹, Lijie Wu¹, Tian Wang^1,², Junlin Liu¹, Fei Li¹, Longquan Jiang^1,², Zhongbo Fan^1,², Yanan Yu^1,², Na Chen¹, Qianqian Sun¹, Qiwen Tan¹, Tian Hua^1,²(

), Zhi-Jie Liu^1,^2,³(

)

¹. iHuman Institute, ShanghaiTech University, Shanghai 201210, China
². School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China
³. Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming 650500, China

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Corresponding Author(s): Tian Hua,Zhi-Jie Liu

Issue Date: 12 March 2024

Cite this article:

Yuxia Wang,Lijie Wu,Tian Wang, et al. Cryo-EM structure of cannabinoid receptor CB1-β-arrestin complex[J]. Protein Cell, 2024, 15(3): 230-234.

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https://academic.hep.com.cn/pac/EN/10.1093/procel/pwad055
https://academic.hep.com.cn/pac/EN/Y2024/V15/I3/230

1	S Ahn, SK Shenoy, LM Luttrell et al. SnapShot: β-Arrestin functions. Cell 2020;182:1362–1362.e1. https://doi.org/10.1016/j.cell.2020.07.034
2	J Bous, A Fouillen, H Orcel et al. Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex. Sci Adv 2022;8:eabo7761. https://doi.org/10.1126/sciadv.abo7761
3	C Cao, X Barros-Alvarez, S Zhang et al. Signaling snapshots of a serotonin receptor activated by the prototypical psychedelic LSD. Neuron 2022;110:3154–3167.e7. https://doi.org/10.1016/j.neuron.2022.08.006
4	D Hilger, M Masureel, BK. Kobilka Structure and dynamics of GPCR signaling complexes. Nat Struct Mol Biol 2018;25:4–12. https://doi.org/10.1038/s41594-017-0011-7
5	T Hua, K Vemuri, M Pu et al. Crystal structure of the human cannabinoid receptor CB1. Cell 2016;167:750–762.e14. https://doi.org/10.1016/j.cell.2016.10.004
6	T Hua, K Vemuri, SP Nikas et al. Crystal structures of agonist- bound human cannabinoid receptor CB1. Nature 2017;547:468–471. https://doi.org/10.1038/nature23272
7	T Hua, X Li, L Wu et al. Activation and signaling mechanism revealed by cannabinoid receptor-Gi complex structures. Cell 2020;180:655–665.e18. https://doi.org/10.1016/j.cell.2020.01.008
8	W Huang, M Masureel, Q Qu et al. Structure of the neurotensin receptor 1 in complex with β-arrestin 1. Nature 2020;579:303–308. https://doi.org/10.1038/s41586-020-1953-1
9	W Jin, S Brown, JP Roche et al. Distinct domains of the CB1 cannabinoid receptor mediate desensitization and internalization. J Neurosci 1999;19:3773–3780. https://doi.org/10.1523/JNEUROSCI.19-10-03773.1999
10	CC Lally, B Bauer, J Selent et al. C-edge loops of arrestin function as a membrane anchor. Nat Commun 2017;8:14258. https://doi.org/10.1038/ncomms14258
11	Y Lee, T Warne, R Nehme et al. Molecular basis of β-arrestin coupling to formoterol-bound beta1-adrenoceptor. Nature 2020;583:862–866. https://doi.org/10.1038/s41586-020-2419-1
12	Z Liu, MR Iyer, G Godlewski et al. Functional selectivity of a biased cannabinoid-1 receptor (CB1R) antagonist. ACS Pharmacol Transl Sci 2021;4:1175–1187. https://doi.org/10.1021/acsptsci.1c00048
13	M Patel, DB Finlay, M. Glass Biased agonism at the cannabinoid receptors - evidence from synthetic cannabinoid receptor agonists. Cell Signal 2021;78:109865. https://doi.org/10.1016/j.cellsig.2020.109865
14	R Santos, O Ursu, A Gaulton et al. A comprehensive map of molecular drug targets. Nat Rev Drug Discov 2017;16:19–34. https://doi.org/10.1038/nrd.2016.230
15	DP Staus, H Hu, MJ Robertson et al. Structure of the M2 muscarinic receptor-β-arrestin complex in a lipid nanodisc. Nature 2020;579:297–302. https://doi.org/10.1038/s41586-020-1954-0

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