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Vol. 9, Issue 12, 3521-3532, December 1998
Center for Molecular Genetics, Department of Biology, University of
California, San Diego, La Jolla, California 92093
A network of interacting proteins has been found that can account
for the spontaneous oscillations in adenylyl cyclase activity that are
observed in homogenous populations of Dictyostelium
cells 4 h after the initiation of development. Previous
biochemical assays have shown that when extracellular adenosine
3',5'-cyclic monophosphate (cAMP) binds to the surface receptor
CAR1, adenylyl cyclase and the MAP kinase ERK2 are
transiently activated. A rise in the internal concentration of cAMP
activates protein kinase A such that it inhibits ERK2 and leads
to a loss-of-ligand binding by CAR1. ERK2 phosphorylates the
cAMP phosphodiesterase REG A that reduces the internal
concentration of cAMP. A secreted phosphodiesterase reduces
external cAMP concentrations between pulses. Numerical solutions to a
series of nonlinear differential equations describing these activities
faithfully account for the observed periodic changes in cAMP. The
activity of each of the components is necessary for the network to
generate oscillatory behavior; however, the model is robust in that
25-fold changes in the kinetic constants linking the activities have
only minor effects on the predicted frequency. Moreover, constant high
levels of external cAMP lead to attenuation, whereas a brief pulse of
cAMP can advance or delay the phase such that interacting cells become entrained.
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