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The Journal of Neuroscience, August 15, 1999, 19(16):6855-6864
Identification of Residues in the N Terminus of  1B Critical
for Inhibition of the Voltage-Dependent Calcium Channel by G 
Carles
Cantí,
Karen M.
Page,
Gary J.
Stephens, and
Annette C.
Dolphin
Department of Pharmacology, University College London, London WC1E
6BT, United Kingdom
To examine the role of the intracellular N terminus in the
G-protein modulation of the neuronal voltage-dependent calcium channel
(VDCC)  1B, we have pursued two routes of investigation. First, we
made chimeric channels between 1B and 1C, the latter not being
modulated by G  subunits. VDCC 1 subunit constructs were
coexpressed with accessory 2 and 2a subunits in
Xenopus oocytes and mammalian (COS-7) cells. G-protein
modulation of expressed 1 subunits was induced by activation of
coexpressed dopamine (D2) receptors with quinpirole in oocytes, or by
cotransfection of G12 subunits in COS-7 cells. For the chimeric
channels, only those with the N terminus of 1B showed any G-protein
modulation; further addition of the first transmembrane domain and I-II
intracellular linker of 1B increased the degree of modulation. To
determine the amino acids within the 1B N terminus, essential for
G-protein modulation, we made mutations of this sequence and identified three amino acids (S48, R52, and R54) within an 11 amino acid sequence
as being critical for G-protein modulation, with I49 being involved to
a lesser extent. This sequence may comprise an essential part of a
complex G-binding site or be involved in its subsequent action.
Key words:
calcium channel; neuronal; G-protein; 1 subunit; G subunit; modulation
Copyright © 1999 Society for Neuroscience 0270-6474/99/19166855-10$05.00/0
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