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J Biol Chem, Vol. 273, Issue 28, 17595-17603, July 10, 1998

Differential Interactions of the C terminus and the Cytoplasmic I-II Loop of Neuronal Ca2+ Channels with G-protein alpha  and beta gamma Subunits
II. EVIDENCE FOR DIRECT BINDING

Taiji Furukawaab, Reiko Miuraa, Yasuo Moricd, Mark Strobeckcd, Kazuyuki Suzukia, Yoshiyasu Ogiharaae, Tomiko Asanof, Rika Morishitaf, Minako Hashiig, Haruhiro Higashidag, Mitsunobu Yoshiih, and Toshihide Nukadaa

From the a Department of Neurochemistry and h Department of Neurophysiology, Tokyo Institute of Psychiatry, 2-1-8 Kamikitazawa, Setagaya-ku, Tokyo 156, the b Department of Internal Medicine, Faculty of Medicine, Teikyo University, 2-11-1 Kaga, Itabashi-ku, Tokyo 173, the c Department of Information Physiology, National Institute for Physiological Sciences, Okazaki, Aichi 444, Japan, the d Institute of Molecular Pharmacology and Biophysics, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267-0828, e New Product Research Laboratories III, Daiichi Pharmaceutical Co., Tokyo R&D Center, 1-16-13 Kita-Kasai, Edogawa-ku, Tokyo 134, the f Department of Biochemistry, Institute for Developmental Research, Aichi Human Service Center, 713-8 Kamiya-cho, Kasugai, Aichi 480-03, and the g Department of Biophysics, Neuroinformation Research Institute, Kanazawa University School of Medicine, 13-1 Takaramachi, Kanazawa, Ishikawa 920, Japan

The present study was designed to obtain evidence for direct interactions of G-protein alpha  (Galpha ) and beta gamma subunits (Gbeta gamma ) with N- (alpha 1B) and P/Q-type (alpha 1A) Ca2+ channels, using synthetic peptides and fusion proteins derived from loop 1 (cytoplasmic loop between repeat I and II) and the C terminus of these channels. For N-type, prepulse facilitation as mediated by Gbeta gamma was impaired when a synthetic loop 1 peptide was applied intracellularly. Receptor agonist-induced inhibition of N-type as mediated by Galpha was also impaired by the loop 1 peptide but only when applied in combination with a C-terminal peptide. For P/Q-type channels, by contrast, the Galpha -mediated inhibition was diminished by application of a C-terminal peptide alone. Moreover, in vitro binding analysis for N- and P/Q-type channels revealed direct interaction of Galpha with C-terminal fusion proteins as well as direct interaction of Gbeta gamma with loop 1 fusion proteins. These findings define loop 1 of N- and P/Q-type Ca2+ channels as an interaction site for Gbeta gamma and the C termini for Galpha .

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.


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