Cortactin modulates cell migration and ring canal morphogenesis during Drosophila oogenesis

Kálmán Somogyi, Pernille Rørth

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Cortactin is a Src substrate that interacts with F-actin and can stimulate actin polymerization by direct interaction with the Arp2/3 complex. We have isolated complete loss-of-function mutants of the single Drosophila cortactin gene. Mutants are viable and fertile, showing that cortactin is not an essential gene. However, cortactin mutants show distinct defects during oogenesis. During oogenesis, Cortactin protein is enriched at the F-actin rich ring canals in the germ line, and in migrating border cells. In cortactin mutants, the ring canals are smaller than normal. A similar phenotype has been observed in Src64 mutants and in mutants for genes encoding Arp2/3 complex components, supporting that these protein products act together to control specific processes in vivo. Cortactin mutants also show impaired border cell migration. This invasive cell migration is guided by Drosophila EGFR and PDGF/VEGF receptor (PVR). We find that accumulation of Cortactin protein is positively regulated by PVR. Also, overexpression of Cortactin can by itself induce F-actin accumulation and ectopic filopodia formation in epithelial cells. We present evidence that Cortactin is one of the factors acting downstream of PVR and Src to stimulate F-actin accumulation. Cortactin is a minor contributor in this regulation, consistent with the cortactin gene not being essential for development.

Original languageEnglish
Pages (from-to)57-64
Number of pages8
JournalMechanisms of Development
Volume121
Issue number1
DOIs
Publication statusPublished - Jan 2004

Keywords

  • Cytoskeleton
  • EMS1
  • Motility

ASJC Scopus subject areas

  • Embryology
  • Developmental Biology

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