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Vol. 11, Issue 8, 2803-2820, August 2000
*Department of Biological Sciences, University of Iowa,
Iowa City, Iowa 52242 Dictyostelium strains in which the gene encoding the
cytoplasmic cAMP phosphodiesterase RegA is inactivated form small
aggregates. This defect was corrected by introducing copies of the
wild-type regA gene, indicating that the defect was
solely the consequence of the loss of the phosphodiesterase. Using a
computer-assisted motion analysis system,
regADepartment of Biochemistry and
Molecular Biology, Baylor College of Medicine, Houston, TX 77030 Department of Molecular and Human Genetics, Baylor
College of Medicine, Houston, TX 77030 §Department of
Biology, University of California, San Diego, La Jolla, CA 92037
mutant cells were found to show
little sense of direction during aggregation. When labeled wild-type
cells were followed in a field of aggregating
regA cells, they also failed to move in an
orderly direction, indicating that signaling was impaired in mutant
cell cultures. However, when labeled regA
cells were followed in a field of aggregating wild-type cells, they
again failed to move in an orderly manner, primarily in the deduced
fronts of waves, indicating that the chemotactic response was also
impaired. Since wild-type cells must assess both the increasing spatial
gradient and the increasing temporal gradient of cAMP in the front of a
natural wave, the behavior of regA cells
was motion analyzed first in simulated temporal waves in the absence of
spatial gradients and then was analyzed in spatial gradients in the
absence of temporal waves. Our results demonstrate that RegA is
involved neither in assessing the direction of a spatial gradient of
cAMP nor in distinguishing between increasing and decreasing temporal
gradients of cAMP. However, RegA is essential for specifically
suppressing lateral pseudopod formation during the response to an
increasing temporal gradient of cAMP, a necessary component of natural
chemotaxis. We discuss the possibility that RegA functions in a network
that regulates myosin phosphorylation by controlling internal cAMP
levels, and, in support of that hypothesis, we demonstrate that myosin
II does not localize in a normal manner to the cortex of
regA cells in an increasing temporal
gradient of cAMP.
Corresponding author.
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