The nullo protein is a component of the actin-myosin network that mediates cellularization in Drosophila melanogaster embryos

Marya A. Postner, Eric F. Wieschaus

Research output: Contribution to journalArticle

40 Scopus citations

Abstract

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-α 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 multinuceate 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-α (sry-α) 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-α protein to the hexagonal network is dependent upon nullo.

Original languageEnglish (US)
Pages (from-to)1863-1873
Number of pages11
JournalJournal of Cell Science
Volume107
Issue number7
StatePublished - Jul 1 1994

All Science Journal Classification (ASJC) codes

  • Cell Biology

Keywords

  • Contractile ring
  • Cytokinesis
  • Drosophila embryo

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