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

Publication ,  Journal Article
Yoshimasa, T; Sibley, DR; Bouvier, M; Lefkowitz, RJ; Caron, MG
Published in: Nature
May 7, 1987

Receptor-mediated activation of both adenylate cyclase and phosphatidylinositide hydrolysis systems occurs through guanine nucleotide regulatory proteins and ultimately leads to specific activation of either cyclic AMP-dependent protein kinase A or Ca2+/phospholipid-dependent protein kinase C. Given the remarkable diversity of agents that influence cellular metabolism through these pathways and the similarities of their components, interactions between the two signalling systems could occur. In fact, stimulation of cells with 12-O-tetradecanoyl phorbol-13-acetate (TPA), a phorbol ester that activates protein kinase C, influences hormone-sensitive adenylate cyclase. In some cells TPA induces desensitization of receptor-mediated stimulation of adenylate cyclase, whereas in others, such as frog erythrocytes, phorbol ester treatment results in increased agonist-stimulated as well as basal, guanine nucleotide- and fluoride ion-stimulated adenylate cyclase activities. We show here that TPA produces phosphorylation of the catalytic unit of adenylate cyclase in frog erythrocytes. Moreover, purified protein kinase C can directly phosphorylate in vitro the catalytic unit of adenylate cyclase purified from bovine brain. These results suggest that phosphorylation of the catalytic unit of adenylate cyclase by protein kinase C may be involved in the phorbol ester-induced enhancement of adenylate cyclase activity. In addition to providing the first direct demonstration of a covalent modification of the catalytic unit of adenylate cyclase, these results provide a potential biochemical mechanism for a regulatory link between the two major transmembrane signalling systems.

Duke Scholars

Published In

Nature

DOI

ISSN

0028-0836

Publication Date

May 7, 1987

Volume

327

Issue

6117

Start / End Page

67 / 70

Location

England

Related Subject Headings

  • Tetradecanoylphorbol Acetate
  • Ranidae
  • Protein Kinase C
  • Phosphorylation
  • Phosphatidylinositols
  • General Science & Technology
  • Erythrocytes
  • Cyclic AMP
  • Cell Communication
  • Animals
 

Citation

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Yoshimasa, T., Sibley, D. R., Bouvier, M., Lefkowitz, R. J., & Caron, M. G. (1987). Cross-talk between cellular signalling pathways suggested by phorbol-ester-induced adenylate cyclase phosphorylation. Nature, 327(6117), 67–70. https://doi.org/10.1038/327067a0
Yoshimasa, T., D. R. Sibley, M. Bouvier, R. J. Lefkowitz, and M. G. Caron. “Cross-talk between cellular signalling pathways suggested by phorbol-ester-induced adenylate cyclase phosphorylation.Nature 327, no. 6117 (May 7, 1987): 67–70. https://doi.org/10.1038/327067a0.
Yoshimasa T, Sibley DR, Bouvier M, Lefkowitz RJ, Caron MG. Cross-talk between cellular signalling pathways suggested by phorbol-ester-induced adenylate cyclase phosphorylation. Nature. 1987 May 7;327(6117):67–70.
Yoshimasa, T., et al. “Cross-talk between cellular signalling pathways suggested by phorbol-ester-induced adenylate cyclase phosphorylation.Nature, vol. 327, no. 6117, May 1987, pp. 67–70. Pubmed, doi:10.1038/327067a0.
Yoshimasa T, Sibley DR, Bouvier M, Lefkowitz RJ, Caron MG. Cross-talk between cellular signalling pathways suggested by phorbol-ester-induced adenylate cyclase phosphorylation. Nature. 1987 May 7;327(6117):67–70.
Journal cover image

Published In

Nature

DOI

ISSN

0028-0836

Publication Date

May 7, 1987

Volume

327

Issue

6117

Start / End Page

67 / 70

Location

England

Related Subject Headings

  • Tetradecanoylphorbol Acetate
  • Ranidae
  • Protein Kinase C
  • Phosphorylation
  • Phosphatidylinositols
  • General Science & Technology
  • Erythrocytes
  • Cyclic AMP
  • Cell Communication
  • Animals