A GFP trap study uncovers the functions of Gilgamesh protein kinase in Drosophila melanogaster spermatogenesis

Authors

  • O.O. Nerusheva,

    1. Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences, Lavrenteva 10, Novosibirsk 630090, Russia
    Search for more papers by this author
  • N.V. Dorogova,

    1. Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences, Lavrenteva 10, Novosibirsk 630090, Russia
    Search for more papers by this author
  • N.V. Gubanova,

    1. Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences, Lavrenteva 10, Novosibirsk 630090, Russia
    Search for more papers by this author
  • O.S. Yudina,

    1. Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences, Lavrenteva 10, Novosibirsk 630090, Russia
    Search for more papers by this author
  • L.V. Omelyanchuk

    Corresponding author
    1. Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences, Lavrenteva 10, Novosibirsk 630090, Russia
    Search for more papers by this author

Tel.: +7 383 305 315. E-mail addresses: ome@bionet.nsc.ru

Abstract

The function of the gene gilgamesh (89B9-12) encoding a casein kinase in Drosophila spermatogenesis was studied. The chimeric Gilgamesh–GFP protein in spermatocytes is cortically located. In the polar and apolar spermatocytes, it concentrates at the terminal ends of the fusome, the organelle that passes through the system of ring canals of the spermatocyte cyst. At the stage of spermatid elongation, the protein associates with the nucleus. A spot of the highest Gilgamesh–GFP concentration in the nucleus co-localizes with γ-tubulin in the basal body. At later stages, Gilgamesh is localized to the individualization complex (IC), leaving the nuclei somewhat before the IC investment cones, as detected by actin binding. The sterile mutation due to the gilgamesh gene leads to the phenotype of scattered nuclei and altered structure of actin cones in the individualizing spermatid cyst. Ultrastructural evidence confirmed defective spermatid individualization due to the mutation. The phylogenetic origin of the protein, and the connection between vesicular trafficking and spermatid individualization, are discussed.

Ancillary