The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Efficient Coupling of Transducin to Monomeric Rhodopsin in a Phospholipid Bilayer
Open accessAbstract
G protein-coupled receptors (GPCRs) are seven transmembrane domain proteins that transduce extracellular signals across the plasma membrane and couple to the heterotrimeric family of G proteins. Like most intrinsic membrane proteins, GPCRs are capable of oligomerization, the function of which has only been established for a few different receptor systems. One challenge in understanding the function of oligomers relates to the inability to separate monomeric and oligomeric receptor complexes in membrane environments. Here we report the reconstitution of bovine rhodopsin, a GPCR expressed in the retina, into an apolipoprotein A-I phospholipid particle, derived from high density lipoprotein (HDL). We demonstrate that rhodopsin, when incorporated into these 10 nm reconstituted HDL (rHDL) particles, is monomeric and functional. Rhodopsin.rHDL maintains the appropriate spectral properties with respect to photoactivation and formation of the active form, metarhodopsin II. Additionally, the kinetics of metarhodopsin II decay is similar between rhodopsin in native membranes and rhodopsin in rHDL particles. Photoactivation of monomeric rhodopsin.rHDL also results in the rapid activation of transducin, at a rate that is comparable with that found in native rod outer segments and 20-fold faster than rhodopsin in detergent micelles. These data suggest that monomeric rhodopsin is the minimal functional unit in G protein activation and that oligomerization is not absolutely required for this process.
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Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
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G Protein–Coupled Receptor Rhodopsin
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Self-citationRhodopsin dimers in native disc membranes
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Self-citationNew Roles for β-Arrestins in Cell Signaling: Not Just for Seven-Transmembrane Receptors
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Full characterization of GPCR monomer–dimer dynamic equilibrium by single molecule imaging
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Allosteric regulation of G protein–coupled receptor activity by phospholipids
Dawaliby, R., Trubbia, C., Delporte, C., Masureel, M., Van Antwerpen, P., Kobilka, B. K., & Govaerts, C. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.1960 · Cited by 304
Hallucinogens and Serotonin 5-HT2A Receptor-Mediated Signaling Pathways
López-Giménez, J. F., & González-Maeso, J. (2017) · Current Topics in Behavioral Neurosciences · doi:10.1007/7854_2017_478 · Cited by 299
Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics
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Metadata
- Authors
- Whorton, M. R., Jastrzebska, B., Park, P. S.-H., Fotiadis, D., Engel, A., Palczewski, K., & Sunahara, R. K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-02
- Volume
- 283
- Issue
- 7
- Pages
- 4387-4394
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2089468762
- Cited by
- 266
- References
- 8
- FWCI
- 8.26
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Whorton, M. R., Jastrzebska, B., Park, P. S.-H., Fotiadis, D., Engel, A., Palczewski, K., & Sunahara, R. K. (2008). Efficient Coupling of Transducin to Monomeric Rhodopsin in a Phospholipid Bilayer. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m703346200
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