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JOURNAL ARTICLES
A cAMP-phosphodiesterase controls PKA-dependent differentiation
G. Shaulsky, D. Fuller, W.F. Loomis
Development 1998 125: 691-699;
G. Shaulsky
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D. Fuller
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W.F. Loomis
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Summary

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.

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JOURNAL ARTICLES
A cAMP-phosphodiesterase controls PKA-dependent differentiation
G. Shaulsky, D. Fuller, W.F. Loomis
Development 1998 125: 691-699;
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JOURNAL ARTICLES
A cAMP-phosphodiesterase controls PKA-dependent differentiation
G. Shaulsky, D. Fuller, W.F. Loomis
Development 1998 125: 691-699;

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