Conserved role of ATP synthase in mammalian cilia

We previously found that ATP synthases localize to male-specific sensory cilia and control the ciliary response by regulating polycystin signalling in Caenorhabditis elegans. Herein, we discovered that the ciliary localization of ATP synthase is evolutionarily conserved in mammals. We showed that the ATP synthase subunit F1 beta is colocalized with the cilia marker acetylated alpha-tubulin in both mammalian renal epithelial cells (MDCK) and normal mouse cholangiocytes (NMCs). Treatment with ATP synthase inhibitor oligomycin impaired ciliogenesis in MDCK cells, and F1 beta was co-immunoprecipitated with PKD2 in mammalian cells. Our study provides evidence for the evolutionarily conserved localization of ATP synthase in cilia from worm to mammals. Defects in ATP synthase can lead to ciliary dysfunction, which may be a potential mechanism of polycystic kidney disease.

Automated summary

The study demonstrates the evolutionarily conserved localization of ATP synthase in cilia from worms to mammals, with the ATP synthase subunit F1 beta colocalized with the cilia marker acetylated alpha-tubulin. Inhibition of ATP synthase with oligomycin affects ciliogenesis, and F1 beta was co-immunoprecipitated with PKD2 in mammalian cells. Defects in ATP synthase can lead to ciliary dysfunction, potentially contributing to polycystic kidney disease.