F-actin-based extensions of the head cyst cell adhere to the maturing spermatids to maintain them in a tight bundle and prevent their premature release in Drosophila testis.
BACKGROUND
In Drosophila, all the 64 clonally derived spermatocytes differentiate in syncytium inside two somatic-origin cyst cells. They elongate to form slender spermatids, which are individualized and then released into the seminal vesicle. During individualization, differentiating spermatids are organized in a tight bundle inside the cyst, which is expected to play an important role in sperm selection. However, actual significance of this process and its underlying mechanism are unclear.


RESULTS
We show that dynamic F-actin-based processes extend from the head cyst cell at the start of individualization, filling the interstitial space at the rostral ends of the maturing spermatid bundle. In addition to actin, these structures contained lamin, beta-catenin, dynamin, myosin VI and several other filopodial components. Further, pharmacological and genetic analyses showed that cytoskeletal stability and dynamin function are essential for their maintenance. Disruption of these F-actin based processes was associated with spermatid bundle disassembly and premature sperm release inside the testis.


CONCLUSIONS
Altogether, our data suggests that the head cyst cell adheres to the maturing spermatid heads through F-actin-based extensions, thus maintaining them in a tight bundle. This is likely to regulate mature sperm release into the seminal vesicle. Overall, this process bears resemblance to mammalian spermiation.
Department of Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai, India. bela@tifr.res.in
Bela S
BS
Desai
Seema
S
Shirolikar
Krishanu
K
Ray
D000199:Actins / Q000378:metabolism*; D000818:Animals; D002448:Cell Adhesion; D002467:Cell Nucleus / Q000378:metabolism; D029721:Drosophila Proteins / Q000378:metabolism; D004331:Drosophila melanogaster / Q000166:cytology* / Q000378:metabolism* / Q000648:ultrastructure; D034281:Dynamins / Q000378:metabolism; D018869:Heat-Shock Response; D006579:Heterozygote; D007150:Immunohistochemistry; D008297:Male; D008870:Microtubules / Q000378:metabolism; D008954:Models, Biological; D009154:Mutation / Q000235:genetics; D011554:Pseudopodia / Q000378:metabolism* / Q000648:ultrastructure; D013087:Spermatids / Q000166:cytology* / Q000648:ultrastructure; D013737:Testis / Q000166:cytology*
D000199:Actins; D029721:Drosophila Proteins; D034281:Dynamins; C439628:shi protein, Drosophila