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Tyrosine-kinase-dependent recruitment of RGS12 to the N-type calcium channel

Author

Listed:
  • Max L. Schiff

    (Mount Sinai School of Medicine)

  • David P. Siderovski

    (University of North Carolina)

  • J. Dedrick Jordan

    (Mount Sinai School of Medicine)

  • Greg Brothers

    (Amgen Research Institute)

  • Bryan Snow

    (Amgen Research Institute)

  • Luc De Vries

    (University of California-San Diego)

  • Daniel F. Ortiz

    (Tufts University School of Medicine)

  • María Diversé-Pierluissi

    (Mount Sinai School of Medicine)

Abstract

γ-Aminobutyric acid (GABA)B receptors couple to Go to inhibit N-type calcium channels in embryonic chick dorsal root ganglion neurons1. The voltage-independent inhibition, mediated by means of a tyrosine-kinase pathway2, is transient and lasts up to 100 seconds. Inhibition of endogenous RGS12, a member of the family of regulators of G-protein signalling, selectively alters the time course of voltage-independent inhibition. The RGS12 protein, in addition to the RGS domain, contains PDZ and PTB domains3. Fusion proteins containing the PTB domain of RGS12 alter the rate of termination of the GABAB signal, whereas the PDZ or RGS domains of RGS12 have no observable effects. Using primary dorsal root ganglion neurons in culture, here we show an endogenous agonist-induced tyrosine-kinase-dependent complex of RGS12 and the calcium channel. These results indicate that RGS12 is a multifunctional protein capable of direct interactions through its PTB domain with the tyrosine-phosphorylated calcium channel. Recruitment of RGS proteins to G-protein effectors may represent an additional mechanism for signal termination in G-protein-coupled pathways.

Suggested Citation

  • Max L. Schiff & David P. Siderovski & J. Dedrick Jordan & Greg Brothers & Bryan Snow & Luc De Vries & Daniel F. Ortiz & María Diversé-Pierluissi, 2000. "Tyrosine-kinase-dependent recruitment of RGS12 to the N-type calcium channel," Nature, Nature, vol. 408(6813), pages 723-727, December.
    • Handle: RePEc:nat:nature:v:408:y:2000:i:6813:d:10.1038_35047093
    DOI: 10.1038/35047093
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