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A more recent version of this article appeared on February 1, 2004
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Submitted on May 1, 2003
Revised on September 10, 2003
Accepted on September 27, 2003
1 Center for Biochemistry, Medical Faculty, University of Cologne, 50931 Köln, Germany
2 Institute of Cell Biology, Ludwig-Maximilians-Universität, 80336 München, Germany
3 School of Life Sciences, Division of Cell and Developmental Biology, University of Dundee, Wellcome Trust Biocentre, Dow Street, Dundee, DD1 5EH, UK
* Corresponding author. E-mail address: schleicher{at}lrz.uni-muenchen.de.
CAP (cyclase associated protein) is an evolutionarily conserved regulator of the G-actin/F-actin ratio and, in yeast, is involved in regulating the adenylyl cyclase activity. We show that cell polarization, F-actin organization and phototaxis are altered in a Dictyostelium CAP knockout mutant. Furthermore, in complementation assays we determined the roles of the individual domains in signaling and regulation of the actin cytoskeleton. We studied in detail the adenylyl cyclase activity and found that the mutant cells have normal levels of the aggregation phase specific adenylyl cyclase (ACA) and that receptor mediated activation is intact. However, cAMP relay which is responsible for the generation of propagating cAMP waves that control the chemotactic aggregation of starving Dictyostelium cells was altered, and the cAMP induced cGMP production was significantly reduced. The data suggest an interaction of CAP with adenylyl cyclase in Dictyostelium and an influence on signaling pathways directly as well as through its function as a regulatory component of the cytoskeleton.
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