Abstract
HUMAN platelet myosin, which is similar to other myosins isolated from non-muscle cells, has a molecular weight of 460,000 and is composed of two heavy chains (200,000) and two different light chains (20,000 and 15,000)1–3. The 20,000 light chain can be phosphorylated by a kinase endogenous to human platelets3. This enzyme, which has been isolated and partially purified4, transfers 32P from γ-32P-ATP to the 20,000 light chain of platelet myosin in the presence of Mg2+. So far, the biological significance of this phosphorylation has been unknown, but we report here that phosphorylation of platelet myosin results in an increase in the actin-activated myosin ATPase activity measured at low ionic strength. Dephosphorylation of phosphorylated myosin results in a decrease in the actin-activated ATPase activity.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Adelstein, R. S., and Conti, M. A., Cold Spring Harb. Symp. quant. Biol., 37, 599–606 (1972).
Pollard, T. D., and Weihing, R. R., Critical Reviews in Biochemistry, 2, 1–65 (CRC, Cleveland, Ohio, 1974).
Andelstein, R. S., Conti, M. A., and Anderson, W., Jr, Proc. natn. Acad. Sci. U.S.A., 70, 3115–3119 (1973).
Adelstein, R. S., Daniel, J. L., Conti, M. A., and Anderson, W., Jr, Proc. Fed. Eur. Biochem. Soc., Ninth FEBS Meeting, Budapest (in the press).
Pires, E., Perry, S. V., and Thomas, M. A., FEBS Lett., 41, 292–296 (9174).
Conti, M. A., and Adelstein, R. S., Fedn Proc., 34, 670a (9175).
Spudich, J. A., and Watt, S., J. biol. Chem., 246, 4866–4871 (1971).
Martin, J. B., and Doty, D. M., Analyt. Chem., 21, 965–967 (1949).
Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., J. biol. Chem., 193, 265–275 (1951).
Fairbanks, G., Steck, T. L., and Wallach, D. F. H., Biochemistry, 10, 2606–2617 (1971).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
ADELSTEIN, R., ANNE CONTI, M. Phosphorylation of platelet myosin increases actin-activated myosin ATPase activity. Nature 256, 597–598 (1975). https://doi.org/10.1038/256597a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/256597a0
This article is cited by
-
EGFR and HER2 activate rigidity sensing only on rigid matrices
Nature Materials (2017)
-
Polarized Distribution of Active Myosin II Regulates Directional Migration of Cultured Olfactory Ensheathing Cells
Scientific Reports (2017)
-
Actin dynamics and competition for myosin monomer govern the sequential amplification of myosin filaments
Nature Cell Biology (2017)
-
Three-dimensional morphogenesis of MDCK cells induced by cellular contractile forces on a viscous substrate
Scientific Reports (2015)
-
Myosin II in mechanotransduction: master and commander of cell migration, morphogenesis, and cancer
Cellular and Molecular Life Sciences (2014)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.