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J. Biol. Chem., Vol. 262, Issue 8, 3918-3926, 03, 1987
CH Berlot, PN Devreotes and JA Spudich
We previously reported (Berlot, C. H., Spudich, J. A., and Devreotes, P. N.
(1985) Cell 43, 307-314) that cAMP stimulation of chemotactically competent
Dictyostelium amoebae causes transient increases in phosphorylation of the
myosin heavy chain and 18,000-dalton light chain in vivo and in vitro. In
this report we investigate the mechanisms involved in these changes in
phosphorylation. In the case of heavy chain phosphorylation, the amount of
substrate available for phosphorylation appears to be the major factor
regulating the in vitro phosphorylation rate. Almost all heavy chain kinase
activity is insoluble in Triton X-100, and the increase in the heavy chain
phosphorylation rate in vitro parallels an increase in Triton insolubility
of myosin. Changes in heavy chain phosphatase activity are not involved in
the changes in the in vitro phosphorylation rate. In the case of light
chain phosphorylation, increases in the vitro phosphorylation rate occur
under conditions where the amount of substrate available for
phosphorylation is constant and phosphatase activity is undetectable,
implicating light chain kinase activation as the means of regulation. The
specificity of the myosin kinases operating in vivo and in vitro was
explored using phosphoamino acid and chymotryptic phosphopeptide analysis.
The light chain is phosphorylated on serine both in vivo and in vitro, and
phosphopeptide maps of the light chain phosphorylated in vivo and in vitro
are indistinguishable. In the case of the heavy chain, both serine and
threonine are phosphorylated in vivo and in vitro, although the
cAMP-stimulated increases in phosphorylation occur primarily on threonine.
Phosphopeptide maps of the heavy chain show that the peptides
phosphorylated in vitro represent a major subset of those phosphorylated in
vivo. The kinetics of the transient increases in myosin phosphorylation
rates observed in vitro can be predicted quantitatively from the in vivo
myosin phosphorylation data assuming that there is a constant phosphatase
activity.
Chemoattractant-elicited increases in Dictyostelium myosin phosphorylation are due to changes in myosin localization and increases in kinase activity
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