Functional analysis of the Drosophila Diaphanous FH protein in early embryonic development

Katayoun Afshar, Bridget Stuart, Steven A. Wasserman

Research output: Contribution to journalArticlepeer-review

135 Scopus citations


The Drosophila Formin Homology (FH) protein Diaphanous has an essential role during cytokinesis. To gain insight into the function of Diaphanous during cytokinesis and explore its role in other processes, we generated embryos deficient for Diaphanous and analyzed three cell-cycle-regulated actin-mediated events during embryogenesis: formation of the metaphase furrow, cellularization and formation of the pole cells. In dia embryos, all three processes are defective. Actin filaments do not organize properly to the metaphase and cellularization furrows and the actin ring is absent from the base of the presumptive pole cells. Furthermore, plasma membrane imaginations that initiate formation of the metaphase furrow and pole cells are missing. Immunolocalization studies of wild-type embryos reveal that Diaphanous localizes to the site where the metaphase furrow is anticipated to form, to the growing tip of cellularization furrows, and to contractile rings. In addition, the dia mutant phenotype reveals a role for Diaphanous in recruitment of myosin II, anillin and Peanut to the cortical region between actin caps. Our findings thus indicate that Diaphanous has a role in actin cytoskeleton organization and is essential for many, if not all, actin-mediated events involving membrane imagination. Based on known biochemical functions of FH proteins, we propose that Diaphanous serves as a mediator between signaling molecules and actin organizers at specific phases of the cell cycle.

Original languageEnglish (US)
Pages (from-to)1887-1897
Number of pages11
Issue number9
StatePublished - May 2000


  • Cellularization
  • Cytoskeleton
  • Diaphanous
  • Drosophila
  • Formin

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology


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