| Literature DB >> 19896897 |
Sergi Ferré1, Amina S Woods, Gemma Navarro, Marisol Aymerich, Carme Lluís, Rafael Franco.
Abstract
The adenosine A(2A)-dopamine D(2) receptor heteromer is one of the most studied receptor heteromers. It has important implications for basal ganglia function and pathology. Recent studies using Bioluminescence and Sequential Resonance Energy Transfer techniques shed light on the role of Ca(2+) in the modulation of the quaternary structure of the A(2A)-D(2) receptor heteromer, which was found to depend on the binding of calmodulin (CaM) to the carboxy-terminus of the A(2A) receptor in the A(2A)-D(2) receptor heteromer. Importantly, the changes in quaternary structure correlate with changes in function. A Ca(2+)/CaM-dependent modulation of MAPK signaling upon agonist treatment could be observed in cells expressing A(2A)-D(2) receptor heteromers. These studies provide a first example of a Ca(2+)-mediated modulation of the quaternary structure and function of a receptor heteromer. Copyright 2009 Elsevier Ltd. All rights reserved.Entities:
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Year: 2009 PMID： 19896897 PMCID： PMC2818424 DOI： 10.1016/j.coph.2009.10.002
Source DB: PubMed Journal: Curr Opin Pharmacol ISSN： 1471-4892 Impact factor: 5.547