The 95F unconventional myosin is required for proper organization of the Drosophila syncytial blastoderm

doi:10.1083/jcb.129.6.1575

This Article

	Full Text (PDF, 5242K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Mermall, V.
	Articles by Miller, K. G.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Mermall, V.
	Articles by Miller, K. G.


Social Bookmarking

	What's this?

ARTICLES

The 95F unconventional myosin is required for proper organization of the Drosophila syncytial blastoderm

V Mermall and KG Miller
Department of Biology, Washington University, St. Louis, Missouri 63130, USA.

The 95F myosin, a class VI unconventional myosin, associates with particles in the cytoplasm of the Drosophila syncytial blastoderm and is required for the ATP- and F-actin-dependent translocation of these particles. The particles undergo a cell cycle-dependent redistribution from domains that surround each nucleus in interphase to transient membrane invaginations that provide a barrier between adjacent spindles during mitosis. When 95F myosin function is inhibited by antibody injection, profound defects in syncytial blastoderm organization occur. This disorganization is seen as aberrant nuclear morphology and position and is suggestive of failures in cytoskeletal function. Nuclear defects correlate with gross defects in the actin cytoskeleton, including indistinct actin caps and furrows, missing actin structures, abnormal spacing of caps, and abnormally spaced furrows. Three- dimensional examination of embryos injected with anti-95F myosin antibody reveals that actin furrows do not invaginate as deeply into the embryo as do normal furrows. These furrows do not separate adjacent mitoses, since microtubules cross over them. These inappropriate microtubule interactions lead to aberrant nuclear divisions and to the nuclear defects observed. We propose that 95F myosin function is required to generate normal actin-based transient membrane furrows. The motor activity of 95F myosin itself and/or components within the particles transported to the furrows by 95F myosin may be required for normal furrows to form.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Webb, R. L., Zhou, M.-N., McCartney, B. M. (2009). A novel role for an APC2-Diaphanous complex in regulating actin organization in Drosophila. Development 136: 1283-1293 [Abstract] [Full Text]
Morrison, J. K., Miller, K. G. (2008). Genetic Characterization of the Drosophila jaguar322 Mutant Reveals That Complete Myosin VI Loss of Function Is Not Lethal. Genetics 179: 711-716 [Abstract] [Full Text]
Sakata, S., Watanabe, Y., Usukura, J., Mabuchi, I. (2007). Characterization of Native Myosin VI Isolated from Sea Urchin Eggs. J Biochem 142: 481-490 [Abstract] [Full Text]
Kiehart, D. P., Crawford, J. M., Montague, R. A. (2007). Quantitative Microinjection of Drosophila Embryos: General Strategy. CSH Protocols 2007: pdb.top5-pdb.top5 [Abstract] [Full Text]
Noguchi, T., Lenartowska, M., Miller, K. G. (2006). Myosin VI Stabilizes an Actin Network during Drosophila Spermatid Individualization. Mol. Biol. Cell 17: 2559-2571 [Abstract] [Full Text]
Royou, A., Field, C., Sisson, J. C., Sullivan, W., Karess, R. (2004). Reassessing the Role and Dynamics of Nonmuscle Myosin II during Furrow Formation in Early Drosophila Embryos. Mol. Biol. Cell 15: 838-850 [Abstract] [Full Text]
Riggs, B., Rothwell, W., Mische, S., Hickson, G. R.X., Matheson, J., Hays, T. S., Gould, G. W., Sullivan, W. (2003). Actin cytoskeleton remodeling during early Drosophila furrow formation requires recycling endosomal components Nuclear-fallout and Rab11. JCB 163: 143-154 [Abstract] [Full Text]
Rogat, A. D., Miller, K. G. (2003). A role for myosin VI in actin dynamics at sites of membrane remodeling during Drosophila spermatogenesis. J. Cell Sci. 115: 4855-4865 [Abstract] [Full Text]
Tzolovsky, G., Millo, H., Pathirana, S., Wood, T., Bownes, M. (2002). Identification and Phylogenetic Analysis of Drosophila melanogaster Myosins. Mol Biol Evol 19: 1041-1052 [Abstract] [Full Text]
Cramer, L. P. (2000). Myosin VI: Roles for a minus End-Directed Actin Motor in Cells. JCB 150: 121-126 [Full Text]
Hicks, J. L., Deng, W.-M., Rogat, A. D., Miller, K. G., Bownes, M. (1999). Class VI Unconventional Myosin is Required for Spermatogenesis in Drosophila. Mol. Biol. Cell 10: 4341-4353 [Abstract] [Full Text]
Raposo, G., Cordonnier, M.-N., Tenza, D., Menichi, B., Dürrbach, A., Louvard, D., Coudrier, E. (1999). Association of Myosin I Alpha with Endosomes and Lysosomes in Mammalian Cells. Mol. Biol. Cell 10: 1477-1494 [Abstract] [Full Text]
Deng, W, Leaper, K, Bownes, M (1999). A targeted gene silencing technique shows that Drosophila myosin VI is required for egg chamber and imaginal disc morphogenesis. J. Cell Sci. 112: 3677-3690 [Abstract]
Rothwell, W., Zhang, C., Zelano, C, Hsieh, T., Sullivan, W (1999). The Drosophila centrosomal protein Nuf is required for recruiting Dah, a membrane associated protein, to furrows in the early embryo. J. Cell Sci. 112: 2885-2893 [Abstract]
Megraw, T., Li, K, Kao, L., Kaufman, T. (1999). The centrosomin protein is required for centrosome assembly and function during cleavage in Drosophila. Development 126: 2829-2839 [Abstract]
Buss, F., Kendrick-Jones, J., Lionne, C., Knight, A. E., Cote, G. P., Paul Luzio, J. (1998). The Localization of Myosin VI at the Golgi Complex and Leading Edge of Fibroblasts and Its Phosphorylation and Recruitment into Membrane Ruffles of A431 Cells after Growth Factor Stimulation. JCB 143: 1535-1545 [Abstract] [Full Text]
Sekiya-Kawasaki, M., Botstein, D., Ohya, Y. (1998). Identification of Functional Connections Between Calmodulin and the Yeast Actin Cytoskeleton. Genetics 150: 43-58 [Abstract] [Full Text]
Lantz, V. A., Miller, K. G. (1998). A Class VI Unconventional Myosin Is Associated with a Homologue of a Microtubule-binding Protein, Cytoplasmic Linker Protein-170, in Neurons and at the Posterior Pole of Drosophila Embryos. JCB 140: 897-910 [Abstract] [Full Text]
Mermall, V., Post, P. L., Mooseker, M. S. (1998). Unconventional Myosins in Cell Movement, Membrane Traffic, and Signal Transduction. Science 279: 527-533 [Abstract] [Full Text]
Nascimento, A. A.C., Amaral, R. G., Bizario, J. C.S., Larson, R. E., Espreafico, E. M. (1997). Subcellular Localization of Myosin-V in the B16 Melanoma Cells, a Wild-type Cell Line for the dilute Gene. Mol. Biol. Cell 8: 1971-1988 [Abstract] [Full Text]
Paddy, M. R., Saumweber, H., Agard, D. A., Sedat, J. W. (1996). Time-resolved, in vivo studies of mitotic spindle formation and nuclear lamina breakdown in Drosophila early embryos. J. Cell Sci. 109: 591-607 [Abstract]