Key result
In vitro motility rate of recombinant myo1b depends on the isoform and calmodulin concentration, with the regulatory domain acting as a rigid lever arm upon calmodulin binding.
The study demonstrates that alternative splicing of Myo1b affects its in vitro motility rate and calmodulin binding properties, with the regulatory domain acting as a rigid lever arm.
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No immediate clinical implications; leaves open Myo1b isoform effects on cardiac motility in vivo.
Lin et al. (2005) studied this question. Recombinant myo1b splice isoforms was evaluated on ATPase activity, motile properties, and calmodulin binding. In vitro motility rate of recombinant myo1b depends on the isoform and calmodulin concentration, with the regulatory domain acting as a rigid lever arm upon calmodulin binding.
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