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. 1979 Jan;76(1):184–188. doi: 10.1073/pnas.76.1.184

Calcium-sensitive regulation of actin-myosin interactions in baby hamster kidney (BHK-21) cells.

M J Yerna, R Dabrowska, D J Hartshorne, R D Goldman
PMCID: PMC382901  PMID: 154671

Abstract

A fraction has been obtained from baby hamster kidney (BHK-21) cells that will stimulate the actin-moderated ATPase (ATP phosphohydrolase, EC 3.6.1.3) activity of both BHK-21 myosin and gizzard smooth muscle myosin. This activation is associated with the specific phosphorylation of the myosin 20,000-dalton light chain. The BHK-21 myosin light chain kinase preparation contains a major protein of approximately 105,000 molecular weight as determined by sodium dodecyl sulfate gel electrophoresis. Both the actin activation and phosphorylation events require the presence of Ca2+ and the so-called modulator or calcium-dependent regulator protein that has been isolated from smooth muscle, brain, and other tissues. On the basis of these results we propose that this kinase system constitutes a Ca2+-dependent regulatory mechanism for myosin-actin interactions in nonmuscle mammalian cells.

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Selected References

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