Journal article
A β4 Isoform-specific Interaction Site in the Carboxyl-terminal Region of the Voltage-dependent Ca2+ Channel α1A Subunit
The Journal of biological chemistry, Vol.273(4), pp.2361-2367
01/23/1998
DOI: 10.1074/jbc.273.4.2361
PMID: 9442082
Abstract
The voltage-gated calcium channel β subunit is a cytoplasmic protein that stimulates activity of the channel-forming subunit, α1, in several ways. Complementary binding sites on α1 and β 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 β subunit. We describe here the characterization in vitro of a second interaction, involving the carboxyl-terminal cytoplasmic domain of α1A and showing specificity for the β4 (and to a lesser extent β2a) isoform. A deletion and chimera approach showed that the carboxyl-terminal region of β4, poorly conserved between β 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.
Details
- Title: Subtitle
- A β4 Isoform-specific Interaction Site in the Carboxyl-terminal Region of the Voltage-dependent Ca2+ Channel α1A Subunit
- Creators
- Denise Walker - INSERM U464, Institut Fédératif Jean Roche, Faculté de Médecine Nord, Bd Pierre Dramard, 13916 Marseille Cedex 20, FranceDelphine Bichet - INSERM U464, Institut Fédératif Jean Roche, Faculté de Médecine Nord, Bd Pierre Dramard, 13916 Marseille Cedex 20, FranceKevin P Campbell - Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City, Iowa 52242Michel De Waard - INSERM U464, Institut Fédératif Jean Roche, Faculté de Médecine Nord, Bd Pierre Dramard, 13916 Marseille Cedex 20, France
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.273(4), pp.2361-2367
- DOI
- 10.1074/jbc.273.4.2361
- PMID
- 9442082
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- Elsevier Inc
- Language
- English
- Date published
- 01/23/1998
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984068387102771
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