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| A beta(4) isoform-specific interaction site in the carboxyl-terminal region of the voltage-dependent Ca2+ channel alpha(1A) subunit |
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| Author(s): Walker D, Bichet D, Campbell KP, De Waard M |
| Source: JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 273 Issue: 4 Pages: 2361-2367 Published: JAN 23 1998 |
| Times Cited: 106 References: 38 |
| 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. |
| Document Type: Article |
| Language: English |
| Reprint Address: De Waard, M (reprint author), Fac Med Nord, Inst Federat Jean Roche, INSERM U464, Bd Pierre Dramard, F-13916 Marseille 20, France |
Addresses:
1. Fac Med Nord, Inst Federat Jean Roche, INSERM U464, F-13916 Marseille 20, France
2. Univ Iowa, Coll Med, Howard Hughes Med Inst, Iowa City, IA 52242 USA |
| Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: YT367 |
| ISSN: 0021-9258 |
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