A cAMP-phosphodiesterase controls PKA-dependent differentiation.
A cAMP-specific phosphodiesterase was found that is stimulated by binding to the regulatory subunit of cAMP-dependent protein kinase, PKA-R, from either Dictyostelium or mammals. The phosphodiesterase is encoded by the regA gene of Dictyostelium, which was recovered in a mutant screen for strains that sporulate in the absence of signals from prestalk cells. The sequence of RegA predicts that it will function as a member of a two-component system. Genetic analyses indicate that inhibition of the phosphodiesterase results in an increase in the activity of PKA, which acts at a check point for terminal differentiation. Conserved components known to affect memory, learning and differentiation in flies and vertebrates suggest that a similar circuitry functions in higher eukaryotes.
Shaulsky
G
G
Center for Molecular Genetics, Department of Biology, University of California San Diego, La Jolla, CA 92093, USA.
Fuller
D
D
Loomis
W F
WF
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism*; D004023:Dictyostelium / Q000166:cytology* / Q000201:enzymology* / Q000235:genetics; D005800:Genes, Fungal; D017125:Genes, Protozoan; D008954:Models, Biological; D009154:Mutation; D010641:Phenotype; D010766:Phosphorylation; D015398:Signal Transduction; D013172:Spores, Fungal / Q000201:enzymology / Q000235:genetics
D017868:Cyclic AMP-Dependent Protein Kinases; D015105:3',5'-Cyclic-AMP Phosphodiesterases