The Drosophila parkin homologue is required for normal mitochondrial dynamics during spermiogenesis

Dev Biol. 2007 Mar 1;303(1):108-20. doi: 10.1016/j.ydbio.2006.10.038. Epub 2006 Nov 10.

Abstract

Drosophila parkin, the ortholog of the human parkin gene, responsible for a familiar form of autosomal recessive juvenile parkinsonism, has been shown previously to be involved in Drosophila male fertility. Loss-of-function mutations in the parkin gene cause failure of spermatid individualization by affecting the proper progression of the actin-based investment cones that assemble in the nuclear region, but fail to translocate in synchrony down the cyst. In parkin mutants, the investment cones are scattered along the post-elongated spermatid bundles and fail to act properly in the process of sperm individualization. Using phase-contrast and electron microscopy analysis, we demonstrate that the parkin spermatids assemble a seemingly normal onion-stage nebenkern, but when the axoneme elongates only one mitochondrial derivative unfurls from the nebenkern. This unique mitochondrial derivative undergoes abnormal shaping and condensation during spermatid elongation. Our results indicate that parkin gene function is necessary for mitochondrial morphogenesis during earlier and later phases of spermiogenesis. The failure of cyst individualization may be due to the sensitivity of investment cone movement to the perturbation of mitochondrial morphology during spermatid elongation.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Animals
  • Crosses, Genetic
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster / embryology*
  • Fluorescent Antibody Technique
  • Male
  • Microscopy, Electron, Transmission
  • Microscopy, Phase-Contrast
  • Mitochondria / physiology*
  • Spermatogenesis / genetics
  • Spermatogenesis / physiology*
  • Spermatozoa / cytology*
  • Spermatozoa / ultrastructure
  • Testis / ultrastructure
  • Ubiquitin-Protein Ligases

Substances

  • Actins
  • Drosophila Proteins
  • Ubiquitin-Protein Ligases
  • park protein, Drosophila