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Originally published as MBC in Press, 10.1091/mbc.E05-02-0103 on April 13, 2005

Vol. 16, Issue 7, 3107-3116, July 2005

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Dynein Light Chain 1 Regulates Dynamin-mediated F-Actin Assembly during Sperm Individualization in Drosophila{boxd}

Anindya Ghosh-Roy *, Bela S. Desai *, and Krishanu Ray

Tata Institute of Fundamental Research, Mumbai 400 005, India

Submitted February 9, 2005; Revised April 4, 2005; Accepted April 5, 2005
Monitoring Editor: Suzanne Pfeffer

Toward the end of spermiogenesis, spermatid nuclei are compacted and the clonally related spermatids individualize to become mature and active sperm. Studies in Drosophila showed that caudal end-directed movement of a microfilament-rich structure, called investment cone, expels the cytoplasmic contents of individual spermatids. F-actin dynamics plays an important role in this process. Here we report that the dynein light chain 1 (DLC1) of Drosophila is involved in two separate cellular processes during sperm individualization. It is enriched around spermatid nuclei during postelongation stages and plays an important role in the dynein-dynactin–dependent rostral retention of the nuclei during this period. In addition, DDLC1 colocalizes with dynamin along investment cones and regulates F-actin assembly at this organelle by retaining dynamin along the cones. Interestingly, we found that this process does not require the other subunits of cytoplasmic dynein-dynactin complex. Altogether, these observations suggest that DLC1 could independently regulate multiple cellular functions and established a novel role of this protein in F-actin assembly in Drosophila.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E05–02–0103) on April 13, 2005.

Abbreviations used: DDLC1, Drosophila dynein light chain 1; NB, nuclear bundle; IC, individualization complex.

{boxd} The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

* These authors contributed equally to this work.

Address correspondence to: Krishanu Ray (krishanu{at}tifr.res.in).




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