Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics
Abstract
The superfamily of G protein-coupled receptors (GPCRs) mediates a wide range of physiological responses and serves as an important category of drug targets. Earlier biochemical and biophysical studies have shown that GPCRs exist temporally in an ensemble of interchanging conformations. Single-molecule techniques are ideally suited to understand the dynamic signaling and conformational complexity of G protein-coupled receptors (GPCRs). Here, we review the progress in single-molecule studies on GPCRs. We introduce the fundamental technical aspects of single-molecule fluorescence. We also survey the methodologies for labeling GPCRs with biophysical probes, particularly fluorescent dyes, and highlight the relevant chemical biology innovations that can be instrumental for studying GPCRs. Finally, we illustrate how the optical techniques and the labeling schemes have been combined to investigate GPCR signaling and dynamics at the single-molecule level.
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GPCRs exist as an ensemble of temporally interchanging conformations.
“GPCRs exist as an ensemble of temporally interchanging conformations [85].”
From G protein-coupled receptors function as cell membrane receptors for the steroid hormone 20-hydroxyecdysone (2020) · cites this paper as [85]
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Cohen, B. E., McAnaney, T. B., Park, E.-S., et al. (2002) · Science · doi:10.1126/science.1069346 · Cited by 381 · see citing works
Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes
Fernández-Suárez, M., Baruah, H., Martínez-Hernández, L., Xie, K. T., Baskin, J. M., Bertozzi, C. R., & Ting, A. Y. (2007) · Nature Biotechnology · doi:10.1038/nbt1355 · Cited by 376 · see citing works
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Zhao, X.-F. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-020-00620-y · Cited by 60 · see citing works
- Authors
- Tian, H., Fürstenberg, A., & Huber, T.
- Affiliations
- Rockefeller University (US)
- Corresponding author
- Huber, Thomas
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2016-06-24
- Volume
- 117
- Issue
- 1
- Pages
- 186-245
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2460402577
- Cited by
- 114
- References
- 671
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 6 · 2023: 9 · 2022: 13 · 2021: 11 · 2020: 10 · 2019: 19 · 2018: 14 · 2017: 20 · 2016: 1
- FWCI
- 1.66
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Chemical Reviews (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Eye Institute (R01 EY012049)
- Novo Nordisk
- Danica Foundation
- Robertson Foundation
- Crowley Family Fund
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- G protein-coupled receptors, single-molecule fluorescence, fluorescent dyes, chemical labeling, G protein-coupled receptor signaling, single-molecule fluorescence microscopy, chemical biology
- MeSH terms
- Fluorescent Dyes, Microscopy, Fluorescence, Signal Transduction, Receptors, G-Protein-Coupled
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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