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Dopamine D1 receptor interaction with arrestin3 in neostriatal neurons
Author(s) -
Macey Tara A.,
Liu Yong,
Gurevich Vsevolod V.,
Neve Kim A.
Publication year - 2005
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2004.02998.x
Subject(s) - colocalization , dopamine receptor d1 , endogenous agonist , agonist , receptor , dopamine receptor , microbiology and biotechnology , dopamine , internalization , chemistry , enzyme linked receptor , dopamine receptor d2 , biology , medicine , endocrinology , biochemistry
Dopamine D1 receptor interactions with arrestins have been characterized using heterologously expressed D1 receptor and arrestins. The purpose of this study was to investigate the interaction of the endogenous D1 receptor with endogenous arrestin2 and 3 in neostriatal neurons. Endogenous arrestin2 and 3 in striatal homogenates bound to the C‐terminus of the D1 receptor in a glutathione‐ S ‐transferase (GST) pulldown assay, with arrestin3 binding more strongly. The D1 C‐terminus and, to a lesser extent, the third cytoplasmic loop also bound purified arrestin2 and 3. In neostriatal neurons, 2, 5, and 20 min agonist treatment increased the colocalization of the D1 receptor and arrestin3 immunoreactivity without altering the colocalization of the D1 receptor and arrestin2. Further, agonist treatment for 5 and 20 min caused translocation of arrestin3, but not arrestin2, to the membrane. The binding of arrestin3, but not arrestin2, to the D1 receptor was increased as assessed by coimmunoprecipitation after agonist treatment for 5 and 20 min. Agonist treatment of neurons induced D1 receptor internalization (35–45%) that was maximal within 2–5 min, a time‐course similar to that of the increase in colocalization of the D1 receptor with arrestin3. These data indicate that the D1 receptor preferentially interacts with arrestin3 in neostriatal neurons.

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