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Cellular expression of the carboxyl terminus of a G protein-coupled receptor kinase attenuates G beta gamma-mediated signaling.

Publication ,  Journal Article
Koch, WJ; Hawes, BE; Inglese, J; Luttrell, LM; Lefkowitz, RJ
Published in: J Biol Chem
February 25, 1994

The beta gamma subunits (G beta gamma) of heterotrimeric G proteins modulate the activity of several signal-transducing effector molecules including G protein-coupled receptor kinases. G beta gamma binds to the carboxyl terminus of the beta-adrenergic receptor kinase (beta ARK) and regulates its activity. To investigate the effect of such a G beta gamma-binding domain on heterologous G beta gamma interactions, various receptors that can stimulate phospholipase C and/or type II adenylate cyclase were coexpressed in COS-7 cells with the carboxyl terminus of beta ARK1. Phosphoinositol hydrolysis in response to activation of receptors that stimulate phospholipase C via Gi beta gamma (alpha 2-adrenergic and M2-muscarinic cholinergic receptors) was markedly inhibited by the coexpressed beta ARK1 polypeptide, whereas that mediated by Gq alpha subunits (alpha 1-adrenergic and M1-muscarinic cholinergic receptors) was unaffected. Increased cellular cAMP levels due to stimulation of receptors and coexpressed adenylate cyclase II displayed marked inhibition in the presence of the beta ARK1 polypeptide. Moreover, inhibition of adenylate cyclase produced by alpha 2-adrenergic receptor stimulation (a Gi alpha-mediated process) was unaffected, indicating that the beta ARK1 polypeptide provides a useful tool for distinguishing between G alpha and G beta gamma pathways.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

February 25, 1994

Volume

269

Issue

8

Start / End Page

6193 / 6197

Location

United States

Related Subject Headings

  • beta-Adrenergic Receptor Kinases
  • Type C Phospholipases
  • Signal Transduction
  • Peptide Fragments
  • Oligodeoxyribonucleotides
  • Molecular Sequence Data
  • GTP-Binding Proteins
  • Enzyme Activation
  • Cyclic AMP-Dependent Protein Kinases
  • Cyclic AMP-Dependent Protein Kinase Type II
 

Citation

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MLA
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Koch, W. J., Hawes, B. E., Inglese, J., Luttrell, L. M., & Lefkowitz, R. J. (1994). Cellular expression of the carboxyl terminus of a G protein-coupled receptor kinase attenuates G beta gamma-mediated signaling. J Biol Chem, 269(8), 6193–6197.
Koch, W. J., B. E. Hawes, J. Inglese, L. M. Luttrell, and R. J. Lefkowitz. “Cellular expression of the carboxyl terminus of a G protein-coupled receptor kinase attenuates G beta gamma-mediated signaling.J Biol Chem 269, no. 8 (February 25, 1994): 6193–97.
Koch WJ, Hawes BE, Inglese J, Luttrell LM, Lefkowitz RJ. Cellular expression of the carboxyl terminus of a G protein-coupled receptor kinase attenuates G beta gamma-mediated signaling. J Biol Chem. 1994 Feb 25;269(8):6193–7.
Koch WJ, Hawes BE, Inglese J, Luttrell LM, Lefkowitz RJ. Cellular expression of the carboxyl terminus of a G protein-coupled receptor kinase attenuates G beta gamma-mediated signaling. J Biol Chem. 1994 Feb 25;269(8):6193–6197.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

February 25, 1994

Volume

269

Issue

8

Start / End Page

6193 / 6197

Location

United States

Related Subject Headings

  • beta-Adrenergic Receptor Kinases
  • Type C Phospholipases
  • Signal Transduction
  • Peptide Fragments
  • Oligodeoxyribonucleotides
  • Molecular Sequence Data
  • GTP-Binding Proteins
  • Enzyme Activation
  • Cyclic AMP-Dependent Protein Kinases
  • Cyclic AMP-Dependent Protein Kinase Type II