Identification of a cardiac isoform of the murine calcium channel alpha1C (Cav1.2-a) subunit and its preferential binding with the beta2 subunit.
We describe a cardiac muscle isoform of the voltage-dependent calcium channel alpha1 subunit, which corresponds to the rabbit ortholog of alpha1C-a (Cav1.2a). We also cloned smooth muscle isoforms alpha1C-b (Cav1.2b) and alpha1C-d (Cav1.2d). Differences among these three isoforms lie within the N-terminal region (exon 1A or 1B), the sixth transmembrane ... segment of domain I (exon 8A or 8B), and the use of exon 10, which forms the intracellular loop between transmembrane domains I and II. Two-hybrid analysis revealed interactions among the three alpha1 isoforms and beta subunits. In vitro overlay and immunoprecipitation analyses revealed preferential binding between alpha1C-a and beta2, which is also expressed at a high level in the heart.
Mesh Terms:
Alternative Splicing, Amino Acid Sequence, Animals, Base Sequence, Calcium Channels, L-Type, Exons, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Muscle, Smooth, Myocardium, Polymerase Chain Reaction, Protein Isoforms, Protein Structure, Tertiary, Protein Subunits, Sequence Deletion, Sequence Homology, Amino Acid
Alternative Splicing, Amino Acid Sequence, Animals, Base Sequence, Calcium Channels, L-Type, Exons, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Muscle, Smooth, Myocardium, Polymerase Chain Reaction, Protein Isoforms, Protein Structure, Tertiary, Protein Subunits, Sequence Deletion, Sequence Homology, Amino Acid
J. Mol. Cell. Cardiol.
Date: Jul. 01, 2006
PubMed ID: 16787652
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