The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.
Full characterization of GPCR monomer–dimer dynamic equilibrium by single molecule imaging
Open accessAbstract
Receptor dimerization is important for many signaling pathways. However, the monomer–dimer equilibrium has never been fully characterized for any receptor with a 2D equilibrium constant as well as association/dissociation rate constants (termed super-quantification). Here, we determined the dynamic equilibrium for the N-formyl peptide receptor (FPR), a chemoattractant G protein–coupled receptor (GPCR), in live cells at 37°C by developing a single fluorescent-molecule imaging method. Both before and after liganding, the dimer–monomer 2D equilibrium is unchanged, giving an equilibrium constant of 3.6 copies/µm2, with a dissociation and 2D association rate constant of 11.0 s−1 and 3.1 copies/µm2s−1, respectively. At physiological expression levels of ∼2.1 receptor copies/µm2 (∼6,000 copies/cell), monomers continually convert into dimers every 150 ms, dimers dissociate into monomers in 91 ms, and at any moment, 2,500 and 3,500 receptor molecules participate in transient dimers and monomers, respectively. Not only do FPR dimers fall apart rapidly, but FPR monomers also convert into dimers very quickly.
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Cites
Partitioning of Lipid-Modified Monomeric GFPs into Membrane Microdomains of Live Cells
Zacharias, D. A., Violin, J. D., Newton, A. C., & Tsien, R. Y. (2002) · Science · doi:10.1126/science.1068539 · Cited by 2,235
Robust single-particle tracking in live-cell time-lapse sequences
Jaqaman, K., Loerke, D., Mettlen, M., Kuwata, H., Grinstein, S., Schmid, S. L., & Danuser, G. (2008) · Nature Methods · doi:10.1038/nmeth.1237 · Cited by 1,970
Hu, C.-D., Chinenov, Y., & Kerppola, T. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00496-3 · Cited by 1,549
Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
Kunishima, N., Shimada, Y., Tsuji, Y., Sato, T., Yamamoto, M., Kumasaka, T., Nakanishi, S., Jingami, H., & Morikawa, K. (2000) · Nature · doi:10.1038/35039564 · Cited by 1,249
GABAB-receptor subtypes assemble into functional heteromeric complexes
Kaupmann, K., Malitschek, B., Schuler, V., Heid, J., Froestl, W., Beck, P., Mosbacher, J., Bischoff, S., Kulik, A., Shigemoto, R., et al. (1998) · Nature · doi:10.1038/25360 · Cited by 1,195
Heterodimerization is required for the formation of a functional GABAB receptor
White, J. H., Wise, A., Main, M. J., Green, A., Fraser, N. J., Disney, G. H., Barnes, A. A., Emson, P., Foord, S. M., & Marshall, F. H. (1998) · Nature · doi:10.1038/25354 · Cited by 1,182
Kusumi, A., Nakada, C., Ritchie, K., Murase, K., Suzuki, K., Murakoshi, H., Kasai, R. S., Kondo, J., & Fujiwara, T. (2005) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.34.040204.144637 · Cited by 1,122
Self-citationGABAB receptors function as a heteromeric assembly of the subunits GABABR1 and GABABR2
Jones, K. A., Borowsky, B., Tamm, J. A., Craig, D. A., Durkin, M. M., Dai, M., Yao, W.-J., Johnson, M., Gunwaldsen, C., Huang, L.-Y., et al. (1998) · Nature · doi:10.1038/25348 · Cited by 1,079
Phospholipids undergo hop diffusion in compartmentalized cell membrane
Fujiwara, T., Ritchie, K., Murakoshi, H., Jacobson, K., & Kusumi, A. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200202050 · Cited by 929
Self-citationHebert, T. E., Moffett, S., Morello, J.-P., Loisel, T. P., Bichet, D. G., Barret, C., & Bouvier, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.27.16384 · Cited by 775
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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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Tian, H., Fürstenberg, A., & Huber, T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00084 · Cited by 114
Busnelli, M., Kleinau, G., Muttenthaler, M., Stoev, S., Manning, M., Bibic, L., Howell, L. A., McCormick, P. J., Di Lascio, S., Braida, D., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00564 · Cited by 67
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Palczewski, K., & Orban, T. (2013) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-062012-170313 · Cited by 44
“…its life cycle (Fichter et al. 2010) or follow a ligand that binds tightly to these receptors (Zhou et al. 2007). allowed investigators to observe a dynamic equilibrium for the N-formyl peptide receptor in live cells, indicating that dimers rapidly fall apart and reassemble (Kasai et al. 2011).”
Background
Metadata
- Authors
- Kasai, R. S., Suzuki, K. G. N., Prossnitz, E. R., Koyama-Honda, I., Nakada, C., Fujiwara, T. K., & Kusumi, A.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2011-02-07
- Volume
- 192
- Issue
- 3
- Pages
- 463-480
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2025951927
- Cited by
- 349
- References
- 60
- FWCI
- 13.52
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Kasai, R. S., Suzuki, K. G. N., Prossnitz, E. R., Koyama-Honda, I., Nakada, C., Fujiwara, T. K., & Kusumi, A. (2011). Full characterization of GPCR monomer–dimer dynamic equilibrium by single molecule imaging. Journal of Cell Biology. https://doi.org/10.1083/jcb.201009128
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