2002
DOI: 10.1046/j.1471-4159.2002.01003.x
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The cytoplasmic tail of the D1A receptor subtype: identification of specific domains controlling dopamine cellular responsiveness

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Cited by 2 publications
(2 citation statements)
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“…As such, one can envision mutating Ser199 5.43 of hD 1 R may restrict the movements of TM5 during the spontaneous isomerization to the R * state and thus impede agonist-independent G protein coupling. In other words, the hD 1 R may possess a CT that offers more steric hindrance to the docking of G s compared to that of hD 5 R, which may account for its lower constitutive activity compared to hD 5 R. In support of this, when we truncated the CT of hD 1 R, we observed an elevation in its agonistindependent activity (Chaar, Jackson, & Tiberi, 2001). Other important residues regulating hD 1 R constitutive activity are shown.…”
Section: Molecular Basis For the Constitutive Activities Of D 1 -Classupporting
confidence: 54%
“…As such, one can envision mutating Ser199 5.43 of hD 1 R may restrict the movements of TM5 during the spontaneous isomerization to the R * state and thus impede agonist-independent G protein coupling. In other words, the hD 1 R may possess a CT that offers more steric hindrance to the docking of G s compared to that of hD 5 R, which may account for its lower constitutive activity compared to hD 5 R. In support of this, when we truncated the CT of hD 1 R, we observed an elevation in its agonistindependent activity (Chaar, Jackson, & Tiberi, 2001). Other important residues regulating hD 1 R constitutive activity are shown.…”
Section: Molecular Basis For the Constitutive Activities Of D 1 -Classupporting
confidence: 54%
“…Other studies also indicated that the cytoplasmic tail of D1-like receptors, especially the N-terminal segment termed as the fourth intracellular loop, played a crucial role in the regulation of the activation of adenylyl cyclase, ligand binding, expression, and G protein coupling properties [ 48 - 52 ]. Members of G protein coupled receptors displayed considerable amino acid sequence conservation within transmembrane domains [ 53 ].…”
Section: Discussionmentioning
confidence: 99%