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Structure of the neurotensin receptor 1 in complex with β-arrestin 1
Open accessAbstract
Arrestin proteins bind to active, phosphorylated G-protein-coupled receptors (GPCRs), thereby preventing G-protein coupling, triggering receptor internalization and affecting various downstream signalling pathways 1,2. Although there is a wealth of structural information detailing the interactions between GPCRs and G proteins, less is known about how arrestins engage GPCRs. Here we report a cryo-electron microscopy structure of full-length human neurotensin receptor 1 (NTSR1) in complex with truncated human β-arrestin 1 (βarr1(ΔCT)). We find that phosphorylation of NTSR1 is critical for the formation of a stable complex with βarr1(ΔCT), and identify phosphorylated sites in both the third intracellular loop and the C terminus that may promote this interaction. In addition, we observe a phosphatidylinositol-4,5-bisphosphate molecule forming a bridge between the membrane side of NTSR1 transmembrane segments 1 and 4 and the C-lobe of arrestin. Compared with a structure of a rhodopsin-arrestin-1 complex, in our structure arrestin is rotated by approximately 85° relative to the receptor. These findings highlight both conserved aspects and plasticity among arrestin-receptor interactions.
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“The structure of the phosphorylated human neurotensin receptor 1 with arrestin reveals a PI(4,5)P2 molecule forming a bridge between the receptor and arrestin [120,121].”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [121]
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Cites
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 46,047
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S. Q., Palovcak, E. J., Armache, J., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,496
UCSF ChimeraX: Meeting modern challenges in visualization and analysis
Goddard, T. D., Huang, C. C., Meng, E. C., Pettersen, E. F., Couch, G. S., Morris, J. H., & Ferrin, T. E. (2018) · Protein Science · doi:10.1002/pro.3235 · Cited by 5,267
MolProbity: More and better reference data for improved all‐atom structure validation
Williams, C. J., Headd, J. J., Moriarty, N. W., Prisant, M. G., Videau, L. L., Deis, L. N., Verma, V., Keedy, D. A., Hintze, B. J., Chen, V. B., et al. (2018) · Protein Science · doi:10.1002/pro.3330 · Cited by 4,599
New tools for automated high-resolution cryo-EM structure determination in RELION-3
Zivanov, J., Nakane, T., Forsberg, B., Kimanius, D., Hagen, W., Lindahl, E., & Scheres, S. (2018) · eLife · doi:10.7554/elife.42166 · Cited by 4,377
Gctf: Real-time CTF determination and correction
Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,417
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Dixon, A. S., Schwinn, M. K., Hall, M. P., Zimmerman, K., Otto, P., Lubben, T. H., Butler, B. L., Binkowski, B. F., Machleidt, T., Kirkland, T. A., et al. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00753 · Cited by 1,405
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Structure and dynamics of GPCR signaling complexes
Hilger, D., Masureel, M., & Kobilka, B. K. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0011-7 · Cited by 969
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Panel, N., Vo, D. D., Hübner, H., Deluigi, M., Pach, S., Bélair, F., Weikert, D., Klenk, C., Hilge, M., Shiva, N., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-74990-1
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Zhou, C., Zhu, C., Wang, X., Yang, Y., & Wei, J. (2026) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2026.179275
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Zheng, C., Lee, S., Gurevich, E. V., & Gurevich, V. V. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.118388
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Eiger, D. S., Smith, J. S., & Rajagopal, S. (2026) · Pharmacological Reviews · doi:10.1016/j.pharmr.2026.100160
Semi-Automated Discovery of Structural Elements Controlling GPCR Function.
Ji, J.-J., & Lyman, E. (2026) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6c01584
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Cecherz, I., Waśkiewicz, J., Dudek, A., Polatyński, D., Wtorek, K., & Piekielna‐Ciesielska, J. (2026) · Pharmaceuticals · doi:10.3390/ph19101550
“The β -arrestins can additionally act as signaling scaffolds, demonstrating that this pathway is not limited to termination of G protein signaling [90,91].”
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Self-citationGupta, V., & Beck‐Sickinger, A. G. (2026) · FEBS Journal · doi:10.1111/febs.70772
Metadata
- Authors
- Huang, W., Masureel, M., Qu, Q., Janetzko, J., Inoue, A., Kato, H. E., Robertson, M. J., Nguyen, K. C., Glenn, J. S., Skiniotis, G., & Kobilka, B. K.
- Affiliations
- Stanford Medicine (US)
- Tohoku University (JP)
- Stanford University (US)
- SLAC National Accelerator Laboratory (US)
- Corresponding author
- Skiniotis, Georgios
- Kobilka, Brian K.
- ORCID
- Venue
- Nature
- Published
- 2020-01-16
- Volume
- 579
- Issue
- 7798
- Pages
- 303-308
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC7100716
- OpenAlex
- W3000145087
- Cited by
- 373
- References
- 58
- Citations by year
- 2026: 45 · 2025: 66 · 2024: 41 · 2023: 63 · 2022: 47 · 2021: 63 · 2020: 46
- FWCI
- 17.62
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institutes of Health (5u19ai109662-05)
- Japan Society for the Promotion of Science (19H03163, 17K08264)
- National Cancer Institute (P30CA124435)
- National Institute of Allergy and Infectious Diseases (U19-AI109662)
- National Institute of Neurological Disorders and Stroke (R01NS028471)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- neurotensin receptor 1, β-arrestin1, G protein-coupled receptors, receptor phosphorylation, phosphatidylinositol 4,5-bisphosphate, receptor internalization, cryo-EM structure
- MeSH terms
- beta-Arrestin 1, Humans, Models, Molecular, Phosphorylation, Receptors, Neurotensin, Cryoelectron Microscopy, Protein Structure, Quaternary, Protein Stability
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