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={Michel Bouvier and Nathalie Guilbault and Hélène Bonin},
  journal={FEBS Letters},
  year={1991},
  volume={279}
}

Protein kinase C‐mediated down‐regulation of β2‐adrenergic receptor and gene expression in rat C6 glioma cells

PKC can regulate β2AR at least two levels: the first being an acute desensitization of receptor function, and the second being a more prolonged repression of receptor gene transcription that in turn results in decreased receptor expression.

Opposing effects of phorbol‐12‐myristate‐13‐acetate, an activator of protein kinase C, on the signaling of structurally related human dopamine D1 and D5 receptors

The finding that cross‐talk between PKC and cAMP pathways can produce such opposite outcomes following the activation of structurally similar D1‐like receptor subtypes is novel and further strengthens the view that D1 and D5 receptors serve distinct functions in the mammalian nervous and endocrine systems.

Protein Kinase C-Mediated Down-Regulation of β1-Adrenergic Receptor Gene Expression in Rat C6 Glioma Cells

It is proposed that the PKC-induced down-regulation of β 1 AR gene transcription in C6 cells is mediated in part by a cAMP response element binding protein-dependent mechanism acting on a novel response element.

Protein kinase c regulation of the adenylyl cyclase system in rat prostatic epithelium

A crosstalk between the PKC and the adenylyl cyclase systems in rat prostatic epithelial cells is supported, due presumably to phosphorylation of both membrane receptors (coupled to Gs) and Gi protein, but not of Gs protein or the adenosine cyclase itself.

Long Term Phorbol Ester Treatment Down-regulates the -Adrenergic Receptor in 3T3-F442A Adipocytes (*)

It is demonstrated that sustained PKC activation exerts a specific control of β3-AR gene expression and is involved, at least in part, in the modulation by insulin of this adrenergic receptor subtype.

Activation of Calcium‐Phospholipid‐Dependent Protein Kinase Enhances Benzodiazepine and Barbiturate Potentiation of the GABAA Receptor

The present results suggest that protein phosphorylation may alter the coupling between the allosteric modulatory sites within the GABAA receptor complex.

Phosphorylation and functional desensitization of the alpha2A-adrenergic receptor by protein kinase C.

Cellular events that result in PKC activation promote phosphorylation of the alpha2AAR and lead to substantial desensitization of receptor function, which represents a mechanism by which rapid crosstalk between the alpha1bAR and other receptors can occur.

Protein Kinase C-Mediated Down-Regulation of b 1-Adrenergic Receptor Gene Expression in Rat C 6 Glioma Cells

It is proposed that the PKC-induced down-regulation of b1AR gene transcription in C6 cells is mediated in part by a cAMP response element binding protein-dependent mechanism acting on a novel response element.

Differential regulation of receptor‐stimulated cyclic adenosine monophosphate production by polyvalent cations in MC3T3‐E1 osteoblasts

Polyvalent cations may either stimulate or inhibit hormone‐mediated cAMP accumulation in osteoblasts and provide a potential explanation for the paradoxical trophic and toxic effects of cations on osteoblast function that occur in vivo under different hormonal conditions.

References

SHOWING 1-10 OF 40 REFERENCES

Tumour promoter uncouples β-adrenergic receptor from adenyl cyclase in mouse epidermis

It is shown that PMA exerts this effect by uncoupling epidermal β-receptors from adenylate cyclase, and that accumulation of cyclic AMP in response to isoprenaline injection is sharply inhibited.

Phorbol ester induces desensitization of adenylate cyclase and phosphorylation of the beta-adrenergic receptor in turkey erythrocytes.

The findings indicate that decreased receptor-Ns coupling is correlated with receptor phosphorylation and that phorbol esters can influence the responsiveness of hormone-sensitive adenylate cyclase in certain cell types.

Modulation of adenylate cyclase of human platelets by phorbol ester. Impairment of the hormone-sensitive inhibitory pathway.

The data obtained suggest than protein kinase C activated by the phorbol ester interferes with the platelet adenylate cyclase system, leading to a specific alteration of the Ni-protein-mediated signal transduction to the adenyatecyclase system.

Cross-talk between cellular signalling pathways suggested by phorbol-ester-induced adenylate cyclase phosphorylation

The first direct demonstration of a covalent modification of the catalytic unit of adenylate cyclase is provided, providing a potential biochemical mechanism for a regulatory link between the two major transmembrane signalling systems.

Activation of protein kinase C potentiates isoprenaline-induced cyclic AMP accumulation in rat pinealocytes

The results suggest that kinase activation is involved and the data provide the first demonstration of a synergistic interaction between Ca2+-phospholipid-dependent protein kinase (protein kinase C) and neurotransmitter-dependent stimulation of cyclic AMP.

Cross‐Talk between Second Messengers

  • M. Bouvier
  • Biology
    Annals of the New York Academy of Sciences
  • 1990
Receptor-mediated stimulation of phosphatidyl-inositides turnover appears to modulate the beta-adrenergic-stimulated adenylyl cyclase activity via protein kinase C-mediated phosphorylation of distinct components of the cAMP production system.