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Papers In Press, published online ahead of print April 2, 2003
Department of Physiology, University of Massachusetts Medical School, Worcester, MA 01655
Corresponding Author: mitsuo.ikebe{at}umassmed.edu
The class III myosin is the most divergent member of the myosin superfamily, having a domain with homology to a protein kinase. However, the function of class III myosin at a molecular level is not known at all and it has been questioned whether it is actually an actin based motor molecule. Here, we showed that human myosin III has an ATPase activity that is significantly activated by actin (20 fold) with Kactin of 112 mM and Vmax of 0.34 s-1, indicating the mechanoenzymatic activity of myosin III. Furthermore, we found that human myosin III has the actin translocating activity (0.11 +/- 0.05 mm/sec) using in vitro actin gliding assay and it moves towards the plus end of actin filaments. Myosin III containing calmodulin as the light chain subunit showed a protein kinase activity and underwent autophosphorylation. The autophosphorylation was the intramolecular process and the sites were at the C-terminal end of the motor domain. Autophosphorylation significantly activated the kinase activity, although it did not affect the ATPase activity. The present study is the first report that clearly demonstrates that the class III myosin is an actin based motor protein having a protein kinase activity.
J. Biol. Chem, 10.1074/jbc.M300757200
Submitted on January 23, 2003
Revised on March 31, 2003
Accepted on April 1, 2003
Determination of human myosin III as a motor protein having a protein kinase activity
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