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Volume 17, Number 4, Issue of February 15, 1997 pp. 1330-1338
Copyright ©1997 Society for Neuroscience

The Intracellular Loop between Domains I and II of the B-Type Calcium Channel Confers Aspects of G-Protein Sensitivity to the E-Type Calcium Channel

Received Oct. 25, 1996; revised Dec. 3, 1996; accepted Dec. 10, 1996.

Karen M. Page, Gary J. Stephens, Nicholas S. Berrow, and Annette C. Dolphin

Department of Pharmacology, Royal Free Hospital School of Medicine, London NW3 2PF, United Kingdom

Neuronal voltage-dependent calcium channels undergo inhibitory modulation by G-protein activation, generally involving both kinetic slowing and steady-state inhibition. We have shown previously that the beta -subunit of neuronal calcium channels plays an important role in this process, because when it is absent, greater receptor-mediated inhibition is observed (). We therefore hypothesized that the calcium channel beta -subunits normally may occlude G-protein-mediated inhibition. Calcium channel beta -subunits bind to the cytoplasmic loop between transmembrane domains I and II of the alpha 1-subunits (). We have examined the hypothesis that this loop is involved in G-protein-mediated inhibition by making chimeras containing the I-II loop of alpha 1B or alpha 1A inserted into alpha 1E (alpha 1EBE and alpha 1EAE, respectively). This strategy was adopted because alpha 1B (the molecular counterpart of N-type channels) and, to a lesser extent, alpha 1A (P/Q-type) are G-protein-modulated, whereas this has not been observed to any great extent for alpha 1E. Although alpha 1B, coexpressed with alpha 2-delta and beta 1b transiently expressed in COS-7 cells, showed both kinetic slowing and steady-state inhibition when recorded with GTPgamma S in the patch pipette, both of which were reversed with a depolarizing prepulse, the chimera alpha 1EBE (and, to a smaller extent, alpha 1EAE) showed only kinetic slowing in the presence of GTPgamma S, and this also was reversed by a depolarizing prepulse. These results indicate that the I-II loop may be the molecular substrate of kinetic slowing but that the steady-state inhibition shown by alpha 1B may involve a separate site on this calcium channel.

Key words: calcium channel; G-protein; beta -subunit; alpha 1B; alpha 1E; modulation




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