Multiple ephrins control cell organization in C. elegans using kinase-dependent and -independent functions of the VAB-1 Eph receptor.
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.
Wang
X
X
Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.
Roy
P J
PJ
Holland
S J
SJ
Zhang
L W
LW
Culotti
J G
JG
Pawson
T
T
D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000166:cytology* / Q000502:physiology*; D029742:Caenorhabditis elegans Proteins; D002450:Cell Communication / Q000502:physiology*; D018797:Cell Cycle Proteins / Q000502:physiology*; D015801:Helminth Proteins / Q000502:physiology*; D007365:Intercellular Junctions / Q000502:physiology; D008565:Membrane Proteins / Q000502:physiology*; D008969:Molecular Sequence Data; D009154:Mutation; D020794:Receptor Protein-Tyrosine Kinases / Q000502:physiology*; D016415:Sequence Alignment; D015398:Signal Transduction
D029742:Caenorhabditis elegans Proteins; D018797:Cell Cycle Proteins; D015801:Helminth Proteins; D008565:Membrane Proteins; D020794:Receptor Protein-Tyrosine Kinases; C111040:vab-1 protein, C elegans