A beta 4 isoform-specific interaction site in the carboxyl-terminal region of the voltage-dependent Ca2+ channel alpha 1A subunit.

The Journal of Biological Chemistry
D WalkerM De Waard

Abstract

The voltage-gated calcium channel beta subunit is a cytoplasmic protein that stimulates activity of the channel-forming subunit, alpha 1, in several ways. Complementary binding sites on alpha 1 and beta have been identified that are highly conserved among isoforms of the two subunits, but this interaction alone does not account for all of the functional effects of the beta subunit. We describe here the characterization in vitro of a second interaction, involving the carboxyl-terminal cytoplasmic domain of alpha 1A and showing specificity for the beta 4 (and to a lesser extent beta 2a) isoform. A deletion and chimera approach showed that the carboxyl-terminal region of beta 4, poorly conserved between beta isoforms, contains the interaction site and plays a role in the regulation of channel inactivation kinetics. This is the first demonstration of a molecular basis for the specificity of functional effects seen for different combinations of these two channel components.

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Citations

Jul 25, 2008·Pflügers Archiv : European journal of physiology·Andriy V DresviannikovAnnette C Dolphin
Aug 31, 2010·Molecules and Cells·Jinhee BaeCheolju Lee
Mar 31, 2007·Neurotherapeutics : the Journal of the American Society for Experimental NeuroTherapeutics·Holly B Kordasiewicz, Christopher M Gomez
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Jan 9, 2003·Proceedings of the National Academy of Sciences of the United States of America·H HibinoF Lesage
Dec 17, 2005·Proceedings of the National Academy of Sciences of the United States of America·Weijun ChengRoberto Coronado
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