The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Formation and dissociation of M 1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules
Open accessAbstract
G-protein–coupled receptors (GPCRs) are the largest family of transmembrane signaling proteins in the human genome. Events in the GPCR signaling cascade have been well characterized, but the receptor composition and its membrane distribution are still generally unknown. Although there is evidence that some members of the GPCR superfamily exist as constitutive dimers or higher oligomers, interpretation of the results has been disputed, and recent studies indicate that monomeric GPCRs may also be functional. Because there is controversy within the field, to address the issue we have used total internal reflection fluorescence microscopy (TIRFM) in living cells to visualize thousands of individual molecules of a model GPCR, the M 1 muscarinic acetylcholine receptor. By tracking the position of individual receptors over time, their mobility, clustering, and dimerization kinetics could be directly determined with a resolution of ~30 ms and ~20 nm. In isolated CHO cells, receptors are randomly distributed over the plasma membrane. At any given time, ~30% of the receptor molecules exist as dimers, and we found no evidence for higher oligomers. Two-color TIRFM established the dynamic nature of dimer formation with M 1 receptors undergoing interconversion between monomers and dimers on the timescale of seconds.
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Self-citationPirenzepine distinguishes between different subclasses of muscarinic receptors
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Self-citationRhodopsin dimers in native disc membranes
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Regulation of μ-opioid receptors: desensitization, phosphorylation, internalization, and tolerance
Williams, J. T., Ingram, S. L., Henderson, G., Chavkin, C., von Zastrow, M., Schulz, S., Koch, T., Evans, C. J., & Christie, M. J. (2013) · Pharmacological Reviews · doi:10.1124/pr.112.005942 · Cited by 802
Full characterization of GPCR monomer–dimer dynamic equilibrium by single molecule imaging
Kasai, R. S., Suzuki, K. G. N., Prossnitz, E. R., Koyama-Honda, I., Nakada, C., Fujiwara, T. K., & Kusumi, A. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201009128 · Cited by 349
Tracking single molecules at work in living cells
Kusumi, A., Tsunoyama, T. A., Hirosawa, K. M., Kasai, R. S., & Fujiwara, T. K. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1558 · Cited by 332
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Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics
Tian, H., Fürstenberg, A., & Huber, T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00084 · Cited by 114
Metadata
- Authors
- Hern, J. A., Baig, A. H., Mashanov, G. I., Birdsall, B., Corrie, J. E. T., Lazareno, S., Molloy, J. E., & Birdsall, N. J. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2010-01-20
- Volume
- 107
- Issue
- 6
- Pages
- 2693-2698
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1973245565
- Cited by
- 383
- References
- 28
- FWCI
- 16.07
- Type
- journal article
- Language
- en
- Open access
- green
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- Hern, J. A., Baig, A. H., Mashanov, G. I., Birdsall, B., Corrie, J. E. T., Lazareno, S., Molloy, J. E., & Birdsall, N. J. M. (2010). Formation and dissociation of M 1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0907915107
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