Abstract
In the DHPRβ1-null zebrafish strain relaxed the lack of β1a results in reduced DHPRα1S membrane expression, in impediment of tetrad formation, and also in the elimination of α1S charge movement (Schredelseker et al., 2005, PNAS). Recently we postulated a model describing the β1a subunit as an allosteric modifier of proper α1S conformation (Schredelseker/Dayal et al., 2009, JBC) and thus enabling full DHPR functionality in skeletal muscle excitation-contraction (EC) coupling.
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