Calcium-sensitive regulation of actin-myosin interactions in baby hamster kidney (BHK-21) cells.
- 1 January 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (1), 184-188
- https://doi.org/10.1073/pnas.76.1.184
Abstract
A fraction was obtained from BHK-21 cells that stimulates 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 MW 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 Ca dependent regulator protein that has been isolated from smooth muscle, brain and other tissues. This kinase system constitutes a Ca2+-dependent regulatory mechanism for myosin-actin interactions in nonmuscle mammalian cells.This publication has 29 references indexed in Scilit:
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