Calcium-mediated modulation of the quaternary structure and function of adenosine A2A-dopamine D2 receptor heteromers

Sergi Ferré; Amina S. Woods; Gemma Navarro; Marisol Aymerich; Carme Lluís; Rafael Franco

doi:10.1016/j.coph.2009.10.002

Calcium-mediated modulation of the quaternary structure and function of adenosine A2A-dopamine D2 receptor heteromers

Sergi Ferré, Amina S. Woods, Gemma Navarro, Marisol Aymerich, Carme Lluís, Rafael Franco

Research output: Contribution to journal › Article › peer-review

21 Scopus citations

Abstract

The adenosine A_2A-dopamine D₂ 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 Ca²⁺ in the modulation of the quaternary structure of the A_2A-D₂ 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-D₂ receptor heteromer. Importantly, the changes in quaternary structure correlate with changes in function. A Ca²⁺/CaM-dependent modulation of MAPK signaling upon agonist treatment could be observed in cells expressing A_2A-D₂ receptor heteromers. These studies provide a first example of a Ca²⁺-mediated modulation of the quaternary structure and function of a receptor heteromer.

Original language	English (US)
Pages (from-to)	67-72
Number of pages	6
Journal	Current Opinion in Pharmacology
Volume	10
Issue number	1
DOIs	https://doi.org/10.1016/j.coph.2009.10.002
State	Published - Feb 2010
Externally published	Yes

ASJC Scopus subject areas

Drug Discovery
Pharmacology

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title = "Calcium-mediated modulation of the quaternary structure and function of adenosine A2A-dopamine D2 receptor heteromers",

abstract = "The adenosine A2A-dopamine D2 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 Ca2+ in the modulation of the quaternary structure of the A2A-D2 receptor heteromer, which was found to depend on the binding of calmodulin (CaM) to the carboxy-terminus of the A2A receptor in the A2A-D2 receptor heteromer. Importantly, the changes in quaternary structure correlate with changes in function. A Ca2+/CaM-dependent modulation of MAPK signaling upon agonist treatment could be observed in cells expressing A2A-D2 receptor heteromers. These studies provide a first example of a Ca2+-mediated modulation of the quaternary structure and function of a receptor heteromer.",

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AU - Ferré, Sergi

AU - Woods, Amina S.

AU - Navarro, Gemma

AU - Aymerich, Marisol

AU - Lluís, Carme

AU - Franco, Rafael

PY - 2010/2

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AB - The adenosine A2A-dopamine D2 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 Ca2+ in the modulation of the quaternary structure of the A2A-D2 receptor heteromer, which was found to depend on the binding of calmodulin (CaM) to the carboxy-terminus of the A2A receptor in the A2A-D2 receptor heteromer. Importantly, the changes in quaternary structure correlate with changes in function. A Ca2+/CaM-dependent modulation of MAPK signaling upon agonist treatment could be observed in cells expressing A2A-D2 receptor heteromers. These studies provide a first example of a Ca2+-mediated modulation of the quaternary structure and function of a receptor heteromer.

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Calcium-mediated modulation of the quaternary structure and function of adenosine A2A-dopamine D2 receptor heteromers

Abstract

ASJC Scopus subject areas

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