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.
Gallagher
P J
PJ
Department of Physiology and Biophysics, Indiana University School of Medicine, Indianapolis 46202-5120, USA.
Stull
J T
JT
D000199:Actins / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000502:physiology; D019556:COS Cells; D008969:Molecular Sequence Data; D009131:Muscle, Smooth, Vascular / Q000737:chemistry / Q000201:enzymology*; D016297:Mutagenesis, Site-Directed; D009219:Myosin-Light-Chain Kinase / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011817:Rabbits; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid
D000199:Actins; D011994:Recombinant Proteins; D009219:Myosin-Light-Chain Kinase