Journal
TRENDS IN PHARMACOLOGICAL SCIENCES
Volume 29, Issue 5, Pages 234-240Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tips.2008.02.004
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Funding
- NEI NIH HHS [R01 EY011500-13, R01 EY011500] Funding Source: Medline
- NIGMS NIH HHS [R01 GM077561-02, R01 GM077561] Funding Source: Medline
- NIMH NIH HHS [R03 MH062651-02] Funding Source: Medline
- NINDS NIH HHS [R01 NS045117-05, R01 NS045117] Funding Source: Medline
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Dimerization is fairly common in the G-protein-coupled receptor (GPCR) superfamily. First attempts to rationalize this phenomenon gave rise to an idea that two receptors in a dinner could be necessary to bind a single molecule of G protein or arrestin. Although GPCRs, G proteins and arrestins were crystallized only in their inactive conformations (in which they do not interact), the structures appeared temptingly compatible with this beautiful model. However, it did not survive the rigors of experimental testing: several recent studies unambiguously demonstrated that one receptor molecule is sufficient to activate a G protein and bind arrestin. Thus, to figure out the biological role of receptor self-association we must focus on other functions of GPCRs at different stages of their functional cycle.
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