TY - JOUR
T1 - Dopamine D2 and D4 receptor heteromerization and its allosteric receptor-receptor interactions
AU - Borroto-Escuela, Dasiel O.
AU - Craenenbroeck, Kathleen Van
AU - Romero-Fernandez, Wilber
AU - Guidolin, Diego
AU - Woods, Amina S.
AU - Rivera, Alicia
AU - Haegeman, Guy
AU - Agnati, Luigi F.
AU - Tarakanov, Alexander O.
AU - Fuxe, Kjell
PY - 2011/1/28
Y1 - 2011/1/28
N2 - Dopamine D2 and D4 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-D4.4 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.
AB - Dopamine D2 and D4 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-D4.4 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.
KW - Allosteric modulation
KW - Dopamine DR receptor
KW - Dopamine DR receptor
KW - G protein-coupled receptors
KW - Heteromerization
KW - Protein-protein interactions.
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U2 - 10.1016/j.bbrc.2010.12.083
DO - 10.1016/j.bbrc.2010.12.083
M3 - Article
C2 - 21184734
AN - SCOPUS:79151483541
VL - 404
SP - 928
EP - 934
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 4
ER -