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Structures of rhodopsin in complex with G-protein-coupled receptor kinase 1
Open accessAbstract
G-protein-coupled receptor (GPCR) kinases (GRKs) selectively phosphorylate activated GPCRs, thereby priming them for desensitization 1. Although it is unclear how GRKs recognize these receptors 2-4, a conserved region at the GRK N terminus is essential for this process 5-8. Here we report a series of cryo-electron microscopy single-particle reconstructions of light-activated rhodopsin (Rho*) bound to rhodopsin kinase (GRK1), wherein the N terminus of GRK1 forms a helix that docks into the open cytoplasmic cleft of Rho*. The helix also packs against the GRK1 kinase domain and stabilizes it in an active configuration. The complex is further stabilized by electrostatic interactions between basic residues that are conserved in most GPCRs and acidic residues that are conserved in GRKs. We did not observe any density for the regulator of G-protein signalling homology domain of GRK1 or the C terminus of rhodopsin. Crosslinking with mass spectrometry analysis confirmed these results and revealed dynamic behaviour in receptor-bound GRK1 that would allow the phosphorylation of multiple sites in the receptor tail. We have identified GRK1 residues whose mutation augments kinase activity and crosslinking with Rho*, as well as residues that are involved in activation by acidic phospholipids. From these data, we present a general model for how a small family of protein kinases can recognize and be activated by hundreds of different GPCRs.
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“We attribute this rise to data qubits leaking into non-computational excited states and anticipate that the inclusion of leakage-removal techniques on data qubits would help to mitigate this rise42,46–48.”
From Suppressing quantum errors by scaling a surface code logical qubit (2023) · cites this paper as [42]
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Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
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Metadata
- Authors
- Chen, Q., Plasencia, M., Li, Z., Mukherjee, S., Patra, D., Chen, C.-L., Klose, T., Yao, X.-Q., Kossiakoff, A. A., Chang, L., Andrews, P. C., & Tesmer, J. J. G.
- Affiliations
- Purdue University West Lafayette (US)
- University of Michigan (US)
- University of Chicago (US)
- Georgia State University (US)
- Corresponding author
- Tesmer, John J. G.
- ORCID
- Venue
- Nature
- Published
- 2021-07-14
- Volume
- 595
- Issue
- 7868
- Pages
- 600-605
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC8607881
- OpenAlex
- W3181632501
- Cited by
- 152
- References
- 96
- Citations by year
- 2026: 25 · 2025: 23 · 2024: 33 · 2023: 28 · 2022: 32 · 2021: 11
- FWCI
- 8.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DigitalCommons@UNO (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- IUScholarWorks (Indiana University) (submittedVersion)
- Funders
- National Science Foundation (1517617)
- American Heart Association (19POST34450193)
- Walther Cancer Foundation
- Purdue University
- National Institutes of Health
- National Heart, Lung, and Blood Institute (R01HL122416, R01HL071818)
- National Cancer Institute (R01CA221289, R01CA254402)
- National Institute of General Medical Sciences (R01GM095832, R01GM105942, R01GM105920, R01GM109896, R01GM117372)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
- Keywords
- rhodopsin, GRK1, GPCR desensitization, receptor phosphorylation, electrostatic interactions, anionic phospholipids
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Cattle, Rhodopsin, Signal Transduction, Protein Structure, Tertiary, Cryoelectron Microscopy, G-Protein-Coupled Receptor Kinase 1
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