TitleThe nullo protein is a component of the actin-myosin network that mediates cellularization in Drosophila melanogaster embryos.
Publication TypeJournal Article
Year of Publication1994
AuthorsPostner, MA, Wieschaus, EF
JournalJ Cell Sci
Volume107 ( Pt 7)
Date Published1994 Jul
KeywordsActin Cytoskeleton, Actins, Animals, Antibodies, Monoclonal, Blastoderm, Cell Cycle, Cell Division, Cytoskeletal Proteins, Drosophila melanogaster, Drosophila Proteins, Embryo, Nonmammalian, Gene Expression, Insect Hormones, Myosins, Protein Biosynthesis, Protein Processing, Post-Translational, Restriction Mapping, Transcription Factors, Transcription, Genetic

After the 13th nuclear division cycle of Drosophila embryogenesis, cortical microfilaments are reorganized into a hexagonal network that drives the subsequent cellularization of the syncytial embryo. Zygotic transcription of the nullo and serendipity-alpha genes is required for normal structuring of the microfilament network. When either gene is deleted, the network assumes an irregular configuration leading to the formation of multinucleate cells. To investigate the role of these genes during cellularization, we have made monoclonal antibodies to both proteins. The nullo protein is present from cycle 13 through the end of cellularization. During cycle 13, it localizes between interphase actin caps and within metaphase furrows. In cellularizing embryos, nullo co-localizes with the actin-myosin network and invaginates along with the leading edge of the plasma membrane. The serendipity-alpha (sry-alpha) protein co-localizes with nullo protein to the hexagonal network but, unlike the nullo protein, it localizes to the sides rather than the vertices of each hexagon. Mutant embryos demonstrate that neither protein translationally regulates the other, but the localization of the sry-alpha protein to the hexagonal network is dependent upon nullo.

Alternate JournalJ. Cell. Sci.