Cortactin colocalizes with filopodial actin and accumulates at IgCAM adhesion sites in Aplysia growth cones

Boris Decourt, Vidhya Munnamalai, Aih Cheun Lee, Lauren Sanchez, Daniel M. Suter

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


Both IgCAMs and the actin cytoskeleton play critical roles in neuronal growth cone motility and guidance. However, it is unclear how IgCAM receptors transduce signals from the plasma membrane to induce actin remodeling. Previous studies have shown that local clustering and immobilization of apCAM, the Aplysia homolog of NCAM, induces Src kinase activity and F-actin polymerization in the peripheral domain of cultured Aplysia bag cell growth cones. Therefore, we wanted to test whether the Src kinase substrate and actin regulator cortactin could be a molecular link between Src activity and actin assembly during apCAM-mediated growth cone guidance. Here, we cloned Aplysia cortactin and showed that it is abundant in the nervous system. Immunostaining of growth cones revealed a strong colocalization of cortactin with F-actin in filopodial bundles and at the leading edge of lamellipodia. Perturbation of the cytoskeleton indicated that cortactin distribution largely depends on actin filaments. Furthermore, active Src colocalized with cortactin in regions of actin assembly, including leading edge and filopodia tips. Finally, we observed that cortactin, like F-actin, localizes to apCAM adhesion sites mediating growth cone guidance. Altogether, these data suggest that cortactin is a mediator of IgCAM-triggered actin assembly involved in growth cone motility and guidance.

Original languageEnglish (US)
Pages (from-to)1057-1068
Number of pages12
JournalJournal of Neuroscience Research
Issue number5
StatePublished - 2009
Externally publishedYes


  • Cortactin
  • F-actin
  • Filopodia
  • Growth cone
  • IgCAM

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience


Dive into the research topics of 'Cortactin colocalizes with filopodial actin and accumulates at IgCAM adhesion sites in Aplysia growth cones'. Together they form a unique fingerprint.

Cite this