A serine point mutation in the adenosine A2AR C-terminal tail reduces receptor heteromerization and allosteric modulation of the dopamine D2R

Author:

Borroto-Escuela Dasiel O.,Marcellino Daniel,Narvaez Manuel,Flajolet Marc,Heintz Nathaniel,Agnati Luigi,Ciruela Francisco,Fuxe Kjell

Funder

Swedish Research Council

Torsten and Ragnar Söderberg Foundation

Hjärnfonden and Marianne and Marcus Wallenberg Foundation

Ministerio de Ciencia e Innovación

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference16 articles.

1. Action of caffeine and theophyllamine on supersensitive dopamine receptors: considerable enhancement of receptor response to treatment with DOPA and dopamine receptor agonists;Fuxe;Med. Biol.,1974

2. Stimulation of high-affinity adenosine A2 receptors decreases the affinity of dopamine D2 receptors in rat striatal membranes;Ferre;Proc. Natl. Acad. Sci. USA,1991

3. Antagonistic A2A/D2 receptor interaction in the striatum as a basis fro adenosine/dopamine interactions in the central nervous system;Fuxe;Drug Dev. Res.,1993

4. Adenosine A2A–dopamine D2 receptor–receptor heteromerization: qualitative and quantitative assessment by fluorescence and bioluminescence energy transfer;Canals;J. Biol. Chem.,2003

5. Oligomerization of adenosine A2A and dopamine D2 receptors in living cells;Kamiya;Biochem. Biophys. Res. Commun.,2003

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