Chemotactic stimulation of aggregation-stage Dictyostelium cells induces rapid changes in energy metabolism, as measured by succinic thiokinase phosphorylation.

In crude mitochondrial fractions of the cellular slime mold Dictyostelium discoideum, a 38-kDa protein can be detected in phosphorylation assays under autophosphorylation conditions in SDS polyacrylamide gels. p38 can be phosphorylated in vitro using either ATP or GTP as phosphoryl donors. After stimulation of aggregation competent cells with the chemoattractant cAMP, p38 phosphorylation pattern changes rapidly. Caffeine, a known inhibitor of cAMP relay in D. discoideum inhibits cAMP induced changes in p38 phosphorylation. The rapid changes in p38 phosphorylation after cAMP stimulation reflect changes in energy metabolism and these changes are most likely mediated by changes in internal calcium concentrations. The mitochondrial localization and other data presented on the characterization of this protein led us to the conclusion that p38 is the alpha subunit of succinic thiokinase. Data showing a correlation between in-vitro p38 phosphorylation and the metabolic state of the cells at the moment of the cell lysis are included.