View Program - 63rd Annual Drosophila Research Conference

Phosducin-like protein 3 (PhLP3) has been shown to possess redox-activity, and it is believed to function as a co-chaperone in the folding of certain cytoskeletal proteins. PhLP3 is very well conserved across the animal kingdom from humans to Drosophila melanogaster. PhLP3’s homolog in Drosophila melanogaster is the uncharacterized CG4511. We find that CG4511 plays a role in the regulation of spermatogenesis in Drosophila melanogaster. A P-element inserted in the 5’ UTR of CG4511 leads to a decrease in its expression, infertility in males homozygous for the P-element and testes that fail to produce mature sperm. Further examination of these CG4511 mutant testes reveals that actin-based individualization cones are absent, as are the needle-like nuclei indicative of mature sperm. Differential interference contrast microscopy and phase contrast microscopy reveal defects in spermatid maturation. Additionally, seminal vesicle size in these CG4511 mutants is severely reduced. Excision of the P-element restores male fertility, spermatogenesis, and seminal vesicle size. Our results suggest the importance of CG4511 in the regulation of spermatogenesis. Given its hypothesized role as a co-chaperone for the folding of cytoskeletal proteins, CG4511 may be required to promote the folding of cytoskeletal proteins needed for spermatogenesis. The absence of actin individualization cones in males homozygous for the CG4511 P-element insert supports this hypothesis. We are currently exploring the hypothesis that CG4511 also regulates microtubule dynamics during spermatogenesis.

Identification of CG4511 as a Novel Regulator of Spermatogenesis