The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation
Open accessAbstract
A major obstacle to understanding the functional importance of dimerization between Class A G protein-coupled receptors (GPCRs) has been the methodological limitation in achieving control of the identity of the components comprising the signaling unit. We have developed a functional complementation assay that enables such control and illustrate it for the human dopamine D2 receptor. The minimal signaling unit, two receptors and a single G protein, is maximally activated by agonist binding to a single protomer, which suggests an asymmetrical activated dimer. Inverse agonist binding to the second protomer enhances signaling, whereas agonist binding to the second protomer blunts signaling. Ligand-independent constitutive activation of the second protomer also inhibits signaling. Thus, GPCR dimer function can be modulated by the activity state of the second protomer, which for a heterodimer may be altered in pathological states. Our novel methodology also makes possible the characterization of signaling from a defined heterodimer unit.
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Cited by
Fribourg, M., Moreno, J. L., Holloway, T., Provasi, D., Baki, L., Mahajan, R., Park, G., Adney, S. K., Hatcher, C., Eltit, J. M., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.055 · Cited by 311
Crystal structure of oligomeric β1-adrenergic G protein–coupled receptors in ligand-free basal state
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Increasing dopamine D2 receptor expression in the adult nucleus accumbens enhances motivation
Trifilieff, P., Feng, B., Urizar, E., Winiger, V, Ward, R. D., Taylor, K. M., Martinez, D., Moore, H., Balsam, P. D., Simpson, E. H., et al. (2013) · Molecular Psychiatry · doi:10.1038/mp.2013.57 · Cited by 206
Self-citationAn update on the physiological and therapeutic relevance of GPCR oligomers
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Metadata
- Authors
- Han, Y., Moreira, I. S., Urizar, E., Weinstein, H., & Javitch, J. A.
- Venue
- Nature Chemical Biology
- Published
- 2009-08-02
- Volume
- 5
- Issue
- 9
- Pages
- 688-695
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W2098876955
- Cited by
- 339
- References
- 59
- FWCI
- 15.48
- Type
- journal article
- Language
- en
- Open access
- green
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