The voltage-dependent calcium channel beta subunit contains two stable interacting domains

Yarden Opatowsky; Orna Chomsky-Hecht; Myoung-Goo Kang; Kevin P Campbell; Joel A Hirsch

doi:10.1074/jbc.M303564200

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The voltage-dependent calcium channel beta subunit contains two stable interacting domains

Journal article

Open access

Peer reviewed

The voltage-dependent calcium channel beta subunit contains two stable interacting domains

Yarden Opatowsky, Orna Chomsky-Hecht, Myoung-Goo Kang, Kevin P Campbell and Joel A Hirsch

The Journal of biological chemistry, Vol.278(52), pp.52323-52332

12/26/2003

DOI: 10.1074/jbc.M303564200

PMID: 14559910

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Abstract

Voltage-dependent calcium channels selectively enable Ca2+ ion movement through cellular membranes. These multiprotein complexes are involved in a wide spectrum of biological processes such as signal transduction and cellular homeostasis. alpha1 is the membrane pore-forming subunit, whereas beta is an intracellular subunit that binds to alpha1, facilitating and modulating channel function. We have expressed, purified, and characterized recombinant beta3 and beta2a using both biochemical and biophysical methods, including electrophysiology, to better understand the beta family's protein structural and functional correlates. Our results indicate that the beta protein is composed of two distinct domains that associate with one another in a stable manner. The data also suggest that the polypeptide regions outside these domains are not structured when beta is not in complex with the channel. In addition, the beta structural core, comprised of just these two domains without other sequences, binds tightly to the alpha interaction domain (AID) motif, a sequence derived from the alpha1 subunit and the principal anchor site of beta. Domain II is responsible for this binding, but domain I enhances it.

Protein Structure, Tertiary

Temperature

Calcium Channels - metabolism

Peptides - chemistry

Signal Transduction

Calcium - metabolism

Electrophoresis, Polyacrylamide Gel

Xenopus laevis

Electrophysiology

Rats

Recombinant Proteins - chemistry

Ions

Amino Acid Motifs

Dose-Response Relationship, Drug

Animals

Calcium Channels - chemistry

Cloning, Molecular

Escherichia coli - metabolism

Polymerase Chain Reaction

Models, Genetic

Calcium Channels, L-Type - metabolism

Circular Dichroism

Calcium Channels, L-Type - chemistry

Cell Line, Transformed

Details

Title: Subtitle: The voltage-dependent calcium channel beta subunit contains two stable interacting domains
Creators: Yarden Opatowsky - Department of Biochemistry, Faculty of Life Sciences, Tel Aviv University, Sherman Bldg., Rm. 621, Ramat Aviv 69978, Israel
Orna Chomsky-Hecht
Myoung-Goo Kang
Kevin P Campbell
Joel A Hirsch
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.278(52), pp.52323-52332
DOI: 10.1074/jbc.M303564200
PMID: 14559910
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: United States
Language: English
Date published: 12/26/2003
Academic Unit: Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
Record Identifier: 9984020856702771

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