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Insulin is present all across the animal kingdom. Its proper release after feeding is of extraordinary importance for nutrient uptake, regulation of metabolism, and growth. We used  Drosophila melanogaster  to shed light on the processes linking dietary leucine intake to insulin secretion. The  Drosophila  genome encodes 8 insulin-like peptides (“Dilps”). Of these, Dilp2 is secreted after the ingestion of a leucine-containing diet. We previously demonstrated that Minidiscs, related to mammalian system-L transporters, acts as a leucine sensor within the Dilp2-secreting insulin-producing cells (“IPCs”) of the brain. Here, we show that a second leucine transporter, JhI-21, of the same family is additionally necessary for proper leucine sensing in the IPCs. Using calcium imaging and  ex-vivo  cultured brains we show that knockdown of  JhI-21  in IPCs causes malfunction of these cells: they are no longer able to sense dietary leucine or to release Dilp2 in a leucine dependent manner.  JhI-21  knockdown in IPCs further causes systemic metabolic defects including defective sugar uptake and altered growth. Finally, we showed that JhI-21 and Minidiscs have no cumulative effect on Dilp2 release. Since system-L transporters are expressed by mammalian β-cells our results could help to better understand the role of these proteins in insulin signaling.

JhI-21 plays a role in Drosophila insulin-like peptide release from larval IPCs via leucine transport