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Evidence that the rate of association of adenosine 3',5'-monophosphate to its chemotactic receptor induces phosphodiesterase activity in Dictyostelium discoideum.

ABSTRACT

Adenosine 3',5'-monophosphate (cyclic AMP) mediates cell aggregation in Dictyostelium discoideum. Cell aggregation is enhanced by pulses of cyclic AMP. Application of pulses of cyclic AMP to cells that were starved only for 1 h (postvegetative cells) induces enzyme activity. One of the enzymes induced by cyclic AMP pulses is phosphodiesterase. We pulsed postvegetative cells with a set of cyclic AMP derivatives that were selected according to certain conformational and physical-chemical properties, and we measured their effect on the induction of phosphodiesterase activity. The cyclic nucleotide specificity for chemotaxis in the aggregative phase was similar to the specificity for phosphodiesterase induction in the postvegetative phase. The shape of the dose-response curves shows a paradox: the activity of a derivative, when applied at receptor-saturating concentrations, is inversely related to its affinity. These results can be explained by the assumption that the response of the chemoreceptor to different cyclic AMP derivatives is proportional to the frequency of associations (rate receptor) and not to the proportion of occupied receptors (occupation receptor). The characteristics of rate receptors and occupation receptors during chemosensory transduction will be discussed.

This article has been cited by other articles:

• Liu, G., Newell, P. C. (1994). Regulation of myosin regulatory light chain phosphorylation via cyclic GMP during chemotaxis of Dictyostelium. J. Cell Sci. 107: 1737-1743 [Abstract]  
• Liu, G, Kuwayama, H, Ishida, S, Newell, P. (1993). The role of cyclic GMP in regulating myosin during chemotaxis of Dictyostelium: evidence from a mutant lacking the normal cyclic GMP response to cyclic AMP. J. Cell Sci. 106: 591-595 [Abstract]