Abstract:
:G protein-coupled receptors (GPCRs) have been found as monomers but also as dimers or higher-order oligomers in cells. The relevance of the monomeric or dimeric receptor state for G protein activation is currently under debate for class A rhodopsin-like GPCRs. Clarification of this issue requires the availability of well defined receptor preparations as monomers or dimers and an assessment of their ligand-binding and G protein-coupling properties. We show by pharmacological and hydrodynamic experiments that purified neurotensin receptor NTS1, a class A GPCR, dimerizes in detergent solution in a concentration-dependent manner, with an apparent affinity in the low nanomolar range. At low receptor concentrations, NTS1 binds the agonist neurotensin with a Hill slope of approximately 1; at higher receptor concentrations, neurotensin binding displays positive cooperativity with a Hill slope of approximately 2. NTS1 monomers activate G alpha q beta(1)gamma(2), whereas receptor dimers catalyze nucleotide exchange with lower affinity. Our results demonstrate that NTS1 dimerization per se is not a prerequisite for G protein activation.
journal_name
Proc Natl Acad Sci U S Aauthors
White JF,Grodnitzky J,Louis JM,Trinh LB,Shiloach J,Gutierrez J,Northup JK,Grisshammer Rdoi
10.1073/pnas.0705312104subject
Has Abstractpub_date
2007-07-17 00:00:00pages
12199-204issue
29eissn
0027-8424issn
1091-6490pii
0705312104journal_volume
104pub_type
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