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• W1826118082 endingPage "347" @default.
• W1826118082 startingPage "339" @default.
• W1826118082 abstract "We compared the phosphorylation and internalization properties of constitutively active <i>alpha</i>-1b adrenergic receptor (AR) mutants carrying mutations in two distant receptor domains, i.e., at A293 in the distal part of the third intracellular loop and at D142 of the DRY motif lying at the end of the third transmembrane domain. For the A293E and A293I mutants the levels of agonist-independent phosphorylation were 150% and 50% higher than those of the wild-type <i>alpha</i>-1b AR, respectively. On the other hand, for the constitutively active D142A and D142T mutants, the basal levels of phosphorylation were similar to those of the wild-type<i>alpha</i>-1b AR and did not appear to be further stimulated by epinephrine. Overexpression of the guanyl nucleotide binding regulatory protein-coupled receptor kinase GRK2 further increases the basal phosphorylation of the A293E mutant, but not that of D142A mutant. Both the wild-type <i>alpha</i>-1b AR and the A293E mutant could undergo β-arrestin-mediated internalization. The epinephrine-induced internalization of the constitutively active A293E mutant was significantly higher than that of the wild-type<i>alpha</i>-1b AR. In contrast, the D142A mutant was impaired in its ability to interact with β-arrestin and to undergo agonist-induced internalization. Interestingly, a double mutant A293E/D142A retained very high constitutive activity and regulatory properties of both the A293E and D142A receptors. These findings demonstrate that two constitutively activating mutations occurring in distant receptor domains of the <i>alpha</i>-1b AR have divergent effects on the regulatory properties of the receptor." @default.
• W1826118082 created "2016-06-24" @default.
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• W1826118082 date "1999-02-01" @default.
• W1826118082 modified "2023-09-26" @default.
• W1826118082 title "Constitutively Active<i>Alpha</i>-1b Adrenergic Receptor Mutants Display Different Phosphorylation and Internalization Features" @default.
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• W1826118082 doi "https://doi.org/10.1124/mol.55.2.339" @default.
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