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Originally published In Press as doi:10.1074/jbc.C000673200 on October 26, 2000

J. Biol. Chem., Vol. 275, Issue 52, 40777-40781, December 29, 2000
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Cross-talk between G-protein and Protein Kinase C Modulation of N-type Calcium Channels Is Dependent on the G-protein beta  Subunit Isoform*

Conan B. CooperDagger §, Michelle I. ArnotDagger , Zhong-Ping FengDagger ||**, Scott E. JarvisDagger Dagger Dagger , Jawed HamidDagger , and Gerald W. ZamponiDagger §§

From the Dagger  Departments of Physiology & Biophysics and Pharmacology & Therapeutics, Neuroscience and Smooth Muscle Research Groups, University of Calgary, Calgary, Alberta T2N 4N1, Canada and || NeuroMed Technologies Inc., Vancouver, British Columbia, Canada

The modulation of N-type calcium current by protein kinases and G-proteins is a factor in the fine tuning of neurotransmitter release. We have previously shown that phosphorylation of threonine 422 in the alpha 1B calcium channel domain I-II linker region resulted in a dramatic reduction in somatostatin receptor-mediated G-protein inhibition of the channels and that the I-II linker consequently serves as an integration center for cross-talk between protein kinase C (PKC) and G-proteins (Hamid, J., Nelson, D., Spaetgens, R., Dubel, S. J., Snutch, T. P., and Zamponi, G. W. (1999) J. Biol. Chem. 274, 6195-6202). Here we show that opioid receptor-mediated inhibition of N-type channels is affected to a lesser extent compared with that seen with somatostatin receptors, hinting at the possibility that PKC/G-protein cross-talk might be dependent on the G-protein subtype. To address this issue, we have examined the effects of four different types of G-protein beta  subunits on both wild type and mutant alpha 1B calcium channels in which residue 422 has been replaced by glutamate to mimic PKC-dependent phosphorylation and on channels that have been directly phosphorylated by protein kinase C. Our data show that phosphorylation or mutation of residue 422 antagonizes the effect of Gbeta 1 on channel activity, whereas Gbeta 2, Gbeta 3, and Gbeta 4 are not affected. Our data therefore suggest that the observed cross-talk between G-proteins and protein kinase C modulation of N-type channels is a selective feature of the Gbeta 1 subunit.

* This work was supported by an operating grant from the Canadian Institutes of Health Research (CIHR) (to G. W. Z.) and through a Scholarship Award from the EJLB Foundation (to G. W. Z.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Recipient of a studentship award from the Heart and Stroke Foundation of Canada.

Recipient of a postdoctoral fellowship award from the Savoy Foundation.

** Recipient of a postdoctoral fellowship from the Natural Science and Engineering Research Council of Canada.

Dagger Dagger Recipient of an Alberta Heritage Foundation for Medical Research (AHFMR) studentship award.

§§ Holds faculty scholarships from the AHFMR and the CIHR and is the Novartis Investigator in Schizophrenia Research. To whom correspondence should be addressed: Dept. of Physiology & Biophysics and Pharmacology & Therapeutics, Neuroscience and Smooth Muscle Research Groups, University of Calgary, 3330 Hospital Drive N. W., Calgary, Alberta T2N 4N1, Canada. Tel.: 403-220-8687; Fax: 403-210-8106; E-mail: zamponi@ucalgary.ca.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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