| Autor: |
Alonso-Llamazares, Ana, Casanova, Emilio, Zamanillo, Daniel, Ovalle, Sergio, Calvo, Pedro, Chinchetru, Miguel A |
| Zdroj: |
Brain Research Bulletin; January 1997, Vol. 42 Issue: 6 p427-430, 4p |
| Abstrakt: |
The third intracellular loop of adrenergic receptors has been implicated in their interaction with guanine nucleotide-binding proteins (G proteins). One of the mechanisms involved in the modulation of receptor function is the phosphorylation of specific residues by intracellular kinases. α1b-Adrenergic receptor is phosphorylated in vitro by cAMP-dependent protein kinase (PKA), although its physiological effect remains to be determined. We have produced fusion proteins formed by glutathione S-transferase and sequences of the third intracellular loop of mouse α1a-, α1b-, and α1d-adrenergic receptor subtypes, and used them as substrates for PKA. Only the fusion protein containing the α1bsequence was phosphorylated in vitro by this kinase. Site-directed mutagenesis of a serine (homologue to serine 278 of the rat sequence, RSS) to an alanine residue precluded phosphorylation by PKA. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
Full Text from ScienceDirect