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Insect osmoregulation is subject to highly sophisticated endocrine control. In  Drosophila , both  Drosophila  kinin and tyramine act on the Malpighian (renal) tubule stellate cell to activate chloride shunt conductance, and so increase the fluid production rate.  Drosophila  kinin is known to act through intracellular calcium, but the mode of action of tyramine is not known. Here, we used a transgenically encoded GFP::apoaequorin translational fusion, targeted to either principal or stellate cells under GAL4/UAS control, to demonstrate that tyramine indeed acts to raise calcium in stellate, but not principal cells. Furthermore, the EC(50) tyramine concentration for half-maximal activation of the intracellular calcium signal is the same as that calculated from previously published data on tyramine-induced increase in chloride flux. In addition, tyramine signalling to calcium is markedly reduced in mutants of  NorpA  (a phospholipase C) and  itpr , the inositol trisphosphate receptor gene, which we have previously shown to be necessary for  Drosophila  kinin signalling. Therefore, tyramine and  Drosophila  kinin signals converge on phospholipase C, and thence on intracellular calcium; and both act to increase chloride shunt conductance by signalling through  itpr . To test this model, we co-applied tyramine and  Drosophila  kinin, and showed that the calcium signals were neither additive nor synergistic. The two signalling pathways thus represent parallel, independent mechanisms for distinct tissues (nervous and epithelial) to control the same aspect of renal function.

A biogenic amine and a neuropeptide act identically: tyramine signals through calcium inDrosophilatubule stellate cells