Drosophila protein kinase D is broadly expressed and a fraction localizes to the Golgi compartment.

Protein kinase D belongs to the subfamily of CaMK. In mammals, three isoforms are known. They have been linked to diverse cellular functions including regulation of cell proliferation, differentiation, apoptosis and motility as well as secretory transport from the trans-Golgi compartment to the plasma membrane. Accordingly, the mammalian PKDs show different intracellular locations, with reported dynamic redistribution, between cytosol, Golgi, plasma membranes and the nucleus, depending on the cell type and exogenous stimuli. The genome of Drosophila melanogaster harbours just one, highly conserved PKD homologue, which is expressed throughout development. PKD mRNA expression during late embryogenesis is restricted to ectodermal derivatives including those involved in cuticle secretion. In imaginal tissues, transcription appears more uniform. PKD protein is detected predominantly in the cytosol with an enrichment in lateral apodemes of late embryos as well as in larval fascicles. In secretory tissues like salivary glands, the protein is concentrated in dotted structures. A PKD-GFP transgene reveals a similar punctuate protein accumulation juxtaposed to a resident Golgi-marker. In cultured cells, transfected Drosophila PKD-GFP colocalizes with a marker of the trans-Golgi compartment like human PKD1-GFP. Similar to the mammalian homologues, Drosophila PKD may be multifunctional including a role in secretory transport in accordance with its subcellular distribution.