Abstract
Unconventional myosin-3B is a single-headed myosin containing an amino-terminal kinase domain. In vitro, we find full length and truncated versions of the molecule to bind the regulatory light chain (RLC) and calmodulin (CaM). The RLC binds to the first IQ-like motif and CaM to the second IQ motif within the neck region of the molecule. Uniquely, we find the RLC to be reversibly exchangeable with CaM in the presence of calcium. Calcium-free conditions favor RLC binding. Exchange of RLC versus CaM to the first IQ motif significantly increases the steady-state ATPase activity in the presence of calcium and modulates the interaction of the molecule with F-actin. This observation shows that the calcium-dependent light chain exchange triggers the activity of human myosin-3B as a molecular motor and suggests that myosin motor function is directly influenced by the set of light chains bound to the neck region.
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