PKC98E Regulates Odorant Responses in Drosophila melanogaster

Drosophila odorant receptors (Ors) are ligand gated ion channels composed of a common receptor subunit Or co-receptor (ORCO) and one of 62 tuning receptor subunits that confer odorant specificity to olfactory neuron responses. Like other sensory systems studied to date, exposing Drosophila olfactory neurons to activating ligands results in reduced responses to subsequent exposures through a process called desensitization. We recently showed that phosphorylation of serine 289 on the common Or subunit ORCO is required for normal peak olfactory neuron responses. Dephosphorylation of this residue occurs on prolonged odorant exposure, and underlies the slow modulation of olfactory neuron responses we term slow desensitiza-tion. Slow desensitization results in the reduction of peak olfactory neuron responses and flattening of dose-response curves, implicating changes in ORCOS289 phosphorylation state as an important modulator of olfactory neuron responses. Here, we report the identification of the primary kinase responsible for ORCOS289 phosphorylation, PKC98E. Antiserum localizes the kinase to the dendrites of the olfactory neurons. Deletion of the kinase from olfactory neurons in the naive state (the absence of prolonged odor exposure) reduces ORCOS289 phosphorylation and reduces peak odorant responses without altering recep-tor localization or expression levels. Genetic rescue with a PKC98E predicted to be constitutively active restores ORCO S289 phosphorylation and olfactory neuron sensitivity to the PKC98E mutants in the naive state. However, the dominant kinase is defective for slow desensitization. Together, these findings reveal that PKC98E is an important regulator of ORCO receptors and olfactory neuron function.

Automated summary

Drosophila odorant receptors consist of a common receptor subunit and tuning receptor subunits that confer odorant specificity to olfactory neuron responses. The phosphorylation state of the common receptor subunit is crucial for olfactory neuron responses, with PKC98E identified as the primary kinase responsible for this phosphorylation. Deletion of PKC98E from olfactory neurons affects peak odorant responses, indicating its importance in regulating olfactory neuron function.