Multiple ephrins control cell organization in C. elegans using kinase-dependent and -independent functions of the VAB-1 Eph receptor

Mol Cell. 1999 Dec;4(6):903-13. doi: 10.1016/s1097-2765(00)80220-8.


Eph receptor (EphR) tyrosine kinases and their ephrin ligands mediate direct cell-to-cell signaling. The C. elegans genome encodes four potential GPI-modified ephrins (EFN-1 to -4) and one EphR (VAB-1). Single and multiple ephrin mutants reveal functions for EFN-1, EFN-2, and EFN-3 in epidermal cell organization that, in aggregate, mirror those of VAB-1. Ephrin mutants have defects in head morphology and enclosure of the embryo by the epidermis and identify ephrin-EphR signaling functions involved in aligning and fusing tail and head epidermal cells, respectively. Biochemical analyses indicate that EFN-1, EFN-2, and EFN-3 jointly activate the VAB-1 tyrosine kinase in vivo. Mutant phenotypes and expression pattern analysis suggest that multiple ephrins are involved in distinct aspects of kinase-dependent and kinase-independent VAB-1 signaling required for proper cell organization during development in C. elegans.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Caenorhabditis elegans / cytology*
  • Caenorhabditis elegans / physiology*
  • Caenorhabditis elegans Proteins*
  • Cell Communication / physiology*
  • Cell Cycle Proteins / physiology*
  • Helminth Proteins / physiology*
  • Intercellular Junctions / physiology
  • Membrane Proteins / physiology*
  • Molecular Sequence Data
  • Mutation
  • Receptor Protein-Tyrosine Kinases / physiology*
  • Sequence Alignment
  • Signal Transduction*


  • Caenorhabditis elegans Proteins
  • Cell Cycle Proteins
  • Helminth Proteins
  • Membrane Proteins
  • Receptor Protein-Tyrosine Kinases
  • vab-1 protein, C elegans