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- W2387969957 abstract "Myosin light chain kinase (MLCK) possesses kinase and non-kinase properties, and both properties play important roles in the regulation of smooth muscle contraction. The purpose is to explore the non-kinase activity of MLCK and to elucidate the molecular mechanism of its activity in regulating contraction. A recombinant GST-fusion protein of the C-terminal domain of MLCK (F6.5) was created. The C-terminal fragment of MLCK was truncated further by deletion of the Ca2+/calmodulin domain (F6.5/D) within this fragment. The MLCK constructs were expressed in E.coli and purified. Using the EnzChek Phosphate Assay and the malachite green method, the unphosphorylated myosin ATPase activity of these recombinant proteins was measured. The results showed that both constructs could stimulate ATPase activity in a dose-dependent manner. However, the extent of ATPase activity was much lower in the F6.5/D construct, suggesting that the amino acid sequence Ala1002-Leu1019 was essential for the non-kinase activity of MLCK. Electron microscopy showed that MLCK(F6.5) could transform inactive myosin filaments to the active form and promote myosin filaments bundle formation." @default.
- W2387969957 created "2016-06-24" @default.
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- W2387969957 date "2007-01-01" @default.
- W2387969957 modified "2023-09-25" @default.
- W2387969957 title "Effect of Non-kinase Activity of Myosin Light Chain Kinase on ATPase Activity of Smooth Muscle Myosin" @default.
- W2387969957 hasPublicationYear "2007" @default.
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