Abstract
The F-actin distribution was studied during pole cell formation in Drosophila embryos using the phalloidin derivative rhodaminyl-lysine- phallotoxin. Nuclei were also stained with 4'-6 diamidine-2- phenylindole dihydrochloride to correlate the pattern seen with the nuclear cycle. The precursors of the pole cells, the polar surface caps, were found to have an F-actin-rich cortex distinct from that of the rest of the embryo surface and an interior cytoplasm that was less intensely stained but brighter than the cytoplasm deeper in the embryo. They were found to divide once without forming true cells and then a second time when cells formed as a result of a meridional and a basal cleavage. Three distinct distributions of the cortical F-actin have been identified during these cleavages. It is concluded that the first division, which cleaves the polar caps but does not separate them from the embryo, involves very different processes from those that lead to the formation of the pole cells. A contractile-ring type of F-actin organization may not be present during the first cleavage but is suggested to occur during the second.
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Selected References
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- Arnold J. M. Cleavage furrow formation in a telolecithal egg (Loligo pealii). I. Filaments in early furrow formation. J Cell Biol. 1969 Jun;41(3):894–904. doi: 10.1083/jcb.41.3.894. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Arnold J. M. Cleavage furrow formation in a telolecithal egg (Loligo pealii). II. Direct evidence for a contraction of the cleavage furrow base. J Exp Zool. 1971 Jan;176(1):73–85. doi: 10.1002/jez.1401760108. [DOI] [PubMed] [Google Scholar]
- Foe V. E., Alberts B. M. Studies of nuclear and cytoplasmic behaviour during the five mitotic cycles that precede gastrulation in Drosophila embryogenesis. J Cell Sci. 1983 May;61:31–70. doi: 10.1242/jcs.61.1.31. [DOI] [PubMed] [Google Scholar]
- Fujiwara K., Pollard T. D. Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow, and mitotic spindle of human cells. J Cell Biol. 1976 Dec;71(3):848–875. doi: 10.1083/jcb.71.3.848. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Giloh H., Sedat J. W. Fluorescence microscopy: reduced photobleaching of rhodamine and fluorescein protein conjugates by n-propyl gallate. Science. 1982 Sep 24;217(4566):1252–1255. doi: 10.1126/science.7112126. [DOI] [PubMed] [Google Scholar]
- Illmensee K., Mahowald A. P., Loomis M. R. The ontogeny of germ plasm during oogenesis in Drosophila. Dev Biol. 1976 Mar;49(1):40–65. doi: 10.1016/0012-1606(76)90257-8. [DOI] [PubMed] [Google Scholar]
- Okada M. Loss of the ability to form pole cells in Drosophila embryos with artificially delayed nuclear arrival at the posterior pole. Prog Clin Biol Res. 1982;85(Pt A):363–372. [PubMed] [Google Scholar]
- Schroeder T. E. Cytokinesis: filaments in the cleavage furrow. Exp Cell Res. 1968 Oct;53(1):272–276. doi: 10.1016/0014-4827(68)90373-x. [DOI] [PubMed] [Google Scholar]
- Schroeder T. E. Dynamics of the contractile ring. Soc Gen Physiol Ser. 1975;30:305–334. [PubMed] [Google Scholar]
- Swanson M. M., Poodry C. A. Pole cell formation in Drosophila melanogaster. Dev Biol. 1980 Mar 15;75(2):419–430. doi: 10.1016/0012-1606(80)90173-6. [DOI] [PubMed] [Google Scholar]
- Szollosi D. Cortical cytoplasmic filaments of cleaving eggs: a structural element corresponding to the contractile ring. J Cell Biol. 1970 Jan;44(1):192–209. doi: 10.1083/jcb.44.1.192. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Verderame M., Alcorta D., Egnor M., Smith K., Pollack R. Cytoskeletal F-actin patterns quantitated with fluorescein isothiocyanate-phalloidin in normal and transformed cells. Proc Natl Acad Sci U S A. 1980 Nov;77(11):6624–6628. doi: 10.1073/pnas.77.11.6624. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Warn R. M., Magrath R. F-actin distribution during the cellularization of the Drosophila embryo visualized with FL-phalloidin. Exp Cell Res. 1983 Jan;143(1):103–114. doi: 10.1016/0014-4827(83)90113-1. [DOI] [PubMed] [Google Scholar]
- Warn R. M., Magrath R. Observations by a novel method of surface changes during the syncytial blastoderm stage of the Drosophila embryo. Dev Biol. 1982 Feb;89(2):540–548. doi: 10.1016/0012-1606(82)90344-x. [DOI] [PubMed] [Google Scholar]
- Warn R. M., Magrath R., Webb S. Distribution of F-actin during cleavage of the Drosophila syncytial blastoderm. J Cell Biol. 1984 Jan;98(1):156–162. doi: 10.1083/jcb.98.1.156. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wieland T., Miura T., Seeliger A. Analogs of phalloidin. D-Abu2-Lys7-phalloin, an F-actin binding analog, its rhodamine conjugate (RLP) a novel fluorescent F-actin-probe, and D-Ala2-Leu7-phalloin, an inert peptide. Int J Pept Protein Res. 1983 Jan;21(1):3–10. [PubMed] [Google Scholar]
- Wulf E., Deboben A., Bautz F. A., Faulstich H., Wieland T. Fluorescent phallotoxin, a tool for the visualization of cellular actin. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4498–4502. doi: 10.1073/pnas.76.9.4498. [DOI] [PMC free article] [PubMed] [Google Scholar]
