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

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Abstract

Phosphorylation of the regulatory light chain of myosin II by myosinlight chain kinase is important for regulating many contractile processes.Smooth muscle myosin light chain kinase has been shown to be associated withboth actin and myosin filaments in vitro and in vivo. In this report wedefine an actin binding region by using molecular deletions to generaterecombinant mutant proteins that were analyzed by co-sedimentation withF-actin. An actin binding region restricted to residues 2-42 in the animoterminus of the rabbit smooth muscle myosin light chain kinase wasidentified.

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Authors and Affiliations

  1. Department of Physiology and Biophysics, Indiana University School of Medicine, Indianapolis, USA

    Patricia J. Gallagher

  2. Department of Physiology, University of Texas Southwestern Medical Center at Dallas, Texas, USA

    James T. Stull

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  1. Patricia J. Gallagher
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  2. James T. Stull
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Gallagher, P.J., Stull, J.T. Localization of an actin binding domain in smooth muscle myosin light chain kinase. Mol Cell Biochem 173, 51–57 (1997). https://doi.org/10.1023/A:1006876318155

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  • DOI: https://doi.org/10.1023/A:1006876318155

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