Localization of an actin binding domain in smooth muscle myosin light chain kinase

Phosphorylation of the regulatory light chain of myosin II by myosin light chain kinase is important for regulating many contractile processes. Smooth muscle myosin light chain kinase has been shown to be associated with both actin and myosin filaments in vitro and in vivo. In this report we define an actin binding region by using molecular deletions to generate recombinant mutant proteins that were analyzed by co-sedimentation with F-actin. An actin binding region restricted to residues 2-42 in the amino terminus of the rabbit smooth muscle myosin light chain kinase was identified.