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Publication : Identification of a cyclic adenosine 3',5'-monophosphate-dependent protein kinase phosphorylation site in the carboxy terminal tail of human D1 dopamine receptor.

First Author  Zamanillo D Year  1995
Journal  Neurosci Lett Volume  188
Issue  3 Pages  183-6
PubMed ID  7609904 Mgi Jnum  J:41602
Mgi Id  MGI:894126 Doi  10.1016/0304-3940(95)11428-y
Citation  Zamanillo D, et al. (1995) Identification of a cyclic adenosine 3',5'-monophosphate-dependent protein kinase phosphorylation site in the carboxy terminal tail of human D1 dopamine receptor. Neurosci Lett 188(3):183-6
abstractText  Each of the dopamine receptor subtypes contains several consensus sites for phosphorylation in their intracellular domains. We have used fusion proteins of the carboxy terminal tail of D1 and D5 dopamine receptors to study the phosphorylation of these proteins by cyclic adenosine 3',5' monophosphate (cAMP)-dependent protein kinase (PKA) and protein kinase C (PKC). The fusion protein of D1 dopamine receptor was efficiently phosphorylated by PKA, but not by PKC. Site-directed mutagenesis of serine 380 to an alanine residue precluded the phosphorylation by the kinase. No phosphorylation of the D5 dopamine receptor fusion protein was observed with either PKA or PKC, which indicates that these receptor subtypes might differ in their mechanisms of regulation.
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