Phorbol‐ester‐induced phosphorylation of the β2‐adrenergic receptor decreases its coupling to Gs

@article{Bouvier1991PhorbolesterinducedPO,
  title={Phorbol‐ester‐induced phosphorylation of the $\beta$2‐adrenergic receptor decreases its coupling to Gs},
  author={M. Bouvier and N. Guilbault and H. Bonin},
  journal={FEBS Letters},
  year={1991},
  volume={279}
}
Phorbol‐esters have been shown to modulated the β‐adrenergie‐stimulated adenylyl cyclase in a number of cell lines. Here, using site directed mutagenesis, we investigate the role of the β‐adrenergic receptor phosphorylation by protein kinase C in this regulatory process. Mutation of the serine‐261, ‐262, ‐344 and ‐345 of the β2‐adrenergic receptor prevented the phorbol‐ester‐induced phosphorylation of the receptor. This mutation also abolished the phorbol‐ester‐induced decrease in high‐affinity… Expand
Phosphorylation and functional desensitization of the alpha2A-adrenergic receptor by protein kinase C.
Differential regulation of receptor‐stimulated cyclic adenosine monophosphate production by polyvalent cations in MC3T3‐E1 osteoblasts
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Cross‐Talk between Second Messengers
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