Àá½Ã¸¸ ±â´Ù·Á ÁÖ¼¼¿ä. ·ÎµùÁßÀÔ´Ï´Ù.
KMID : 0578320100300030185
Molecules and Cells
2010 Volume.30 No. 3 p.185 ~ p.191
Interaction of T-Type Calcium Channel CaV3.3 with the ¥â-Subunit
Bae Jin-Hee

Suh Eui-Jin
Lee Cheol-ju
Abstract
The ¥â-subunit of high-voltage-activated (HVA) calcium channels is essential for the regulation of expression and gating. On the other hand, various reports have suggested that ¥â subunits play no role in the regulation of low-voltage-activated T-type channels. In addition there has been no clear demonstration of a physical interaction between the ¥â-subunit of T-type channel with ¥â-subunit. In this study, we systematically investigated the interaction between CaV¥á and CaV¥â. The four CaV¥â isoforms were expressed in a bacterial system and purified into homogeneity, whereas the ten types of CaV¥á alpha interaction domain (AID) peptides were chemically synthesized. All possible combinations of CaV¥á and CaV¥â were then tested for by in vitro immunoassays. We describe here the identification of a new interaction between CaV3.3 and CaV¥â proteins. This interaction is of low affinity compared to that between the AID of the HVA ¥â-subunit and the alpha-binding pocket (ABP) site of the ¥â-subunit. The AID peptide of HVA channel exerted no effect on the CaV3.3-CaV¥â interaction, thus demonstrating that another site not in the ABP of CaV¥â protein played a role in binding with CaV3.3. This is the first demonstration of an ¥á-¥â subunit interaction in a T-type calcium channel.
KEYWORD
calcium channel, CaV3.3, ¥â subunit
FullTexts / Linksout information
Listed journal information
SCI(E) MEDLINE ÇмúÁøÈïÀç´Ü(KCI)