C. elegans enabled exhibits novel interactions with N-WASP, Abl, and cell-cell junctions

Mark Sheffield, Timothy Loveless, Jeff Hardin, Jonathan Pettitt

Research output: Contribution to journalArticle

39 Citations (Scopus)


Ena/VASP proteins are associated with cell-cell junctions in cultured mammalian cells [1] and Drosophila epithelia [2,3], but they have only been extensively studied at the leading edges of migratory fibroblasts, where they modulate the protrusion of the leading edge [4]. They act by regulating actin-filament geometry, antagonizing the effects of actin-capping protein [5]. Embryos lacking the C. elegans Ena/VASP, UNC-34, display subtle defects in the leading edges of migrating epidermal cells but undergo normal epidermal morphogenesis. In contrast, embryos lacking both UNC-34 and the C. elegans N-WASP homolog have severe defects in epidermal morphogenesis, suggesting that they have parallel roles in coordinating cell behavior. GFP-tagged UNC-34 localizes to the leading edges of migrating epidermal cells, becoming redistributed to new junctions that form during epidermal-sheet sealing. Consistent with this, UNC-34 contributes to the formation of cadherin-based junctions. The junctional localization of UNC-34 is independent of proteins involved in Ena/VASP localization in other experimental systems; instead, junctional distribution depends upon the junctional protein AJM-1. We also show that Abelson tyrosine kinase, a major regulator of Enabled in Drosophila, is not required for UNC-34/Ena function in epithelia. Instead, our data suggest that Abelson kinase acts in parallel to UNC-34/Ena, antagonizing its function.

Original languageEnglish
Pages (from-to)1791-1796
Number of pages6
JournalCurrent Biology
Issue number20
Publication statusPublished - 23 Oct 2007


  • ENA/VASP proteins
  • actin polymerization
  • fibroblast motility
  • spatial control
  • Abelson Kinase
  • migration
  • morphogenesis
  • drosophila
  • cytoskeleton
  • complex


Dive into the research topics of 'C. elegans enabled exhibits novel interactions with N-WASP, Abl, and cell-cell junctions'. Together they form a unique fingerprint.

Cite this