Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 404, Issue 4, Pages 928-934Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2010.12.083
Keywords
Dopamine D2R receptor; Dopamine D4R receptor; Heteromerization; G protein-coupled receptors; Allosteric modulation; Protein-protein interactions
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Funding
- Swedish Research Council [04X-715]
- Hjarnfonden, Torsten and Ragnar Soderberg
- M.M. Wallenberg Foundation
- FWO
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Dopamine D-2 and D-4 receptors partially codistribute in the dorsal striatum and appear to play a fundamental role in complex behaviors and motor function. The discovery of D2R-D4.xR (D4.2R, D4.4R or D4.7R) heteromers has been made in cellular models using co-immunoprecipitation, in situ Proximity Ligation Assays and BRET1 techniques with the D2R and D4.7R receptors being the least effective in forming heteromers. Allosteric receptor-receptor interactions in D2R-D4.2R and D2R-D-4.4 R heteromers were observed using the MAPK assays indicating the existence of an enhancing allosteric receptor-receptor interaction in the corresponding heteromers between the two orthosteric binding sites. The bioinformatic predictions suggest the existence of a basic set of common triplets (ALQ and LRA) in the two participating receptors that may contribute to the receptor-receptor interaction interfaces. (C) 2010 Elsevier Inc. All rights reserved.
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