Key result
ZnT-1 inhibits the L-type calcium channel by interacting with its beta-subunit, which decreases the trafficking of the pore-forming alpha(1)-subunit to the surface membrane.
This study elucidates the molecular mechanism by which ZnT-1 inhibits L-type calcium channels, showing it depends on interaction with the beta-subunit to reduce alpha(1)-subunit surface expression.
The L-type calcium channel (LTCC) has a variety of physiological roles that are critical for the proper function of many cell types and organs. Recently, a member of the zinc-regulating family of proteins, ZnT-1, was recognized as an endogenous inhibitor of the LTCC, but its mechanism of action has not been elucidated. In the present study, using two-electrode voltage clamp recordings in Xenopus oocytes, we demonstrate that ZnT-1-mediated inhibition of the LTCC critically depends on the presence of the LTCC regulatory beta-subunit. Moreover, the ZnT-1-induced inhibition of the LTCC current is also abolished by excess levels of the beta-subunit. An interaction between ZnT-1 and the beta-subunit, as demonstrated by co-immunoprecipitation and by fluorescence resonance energy transfer, is consistent with this result. Using surface biotinylation and total internal reflection fluorescence microscopy in HEK293 cells, we show a ZnT-1-dependent decrease in the surface expression of the pore-forming alpha(1)-subunit of the LTCC. Similarly, a decrease in the surface expression of the alpha(1)-subunit is observed following up-regulation of the expression of endogenous ZnT-1 in rapidly paced cultured cardiomyocytes. We conclude that ZnT-1-mediated inhibition of the LTCC is mediated through a functional interaction of ZnT-1 with the LTCC beta-subunit and that it involves a decrease in the trafficking of the LTCC alpha(1)-subunit to the surface membrane.
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Levy et al. (2009) studied this question. ZnT-1 was evaluated on Mechanism of LTCC inhibition. ZnT-1 inhibits the L-type calcium channel by interacting with its beta-subunit, which decreases the trafficking of the pore-forming alpha(1)-subunit to the surface membrane.
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