aph-2 encodes a novel extracellular protein required for GLP-1-mediated signaling.
In animal development, numerous cell-cell interactions are mediated by the GLP-1/LIN-12/NOTCH family of transmembrane receptors. These proteins function in a signaling pathway that appears to be conserved from nematodes to humans. We show here that the aph-2 gene is a new component of the GLP-1 signaling pathway in the early Caenorhabditis elegans embryo, and that proteins with sequence similarity to the APH-2 protein are found in Drosophila and vertebrates. During the GLP-1-mediated cell interactions in the C. elegans embryo, APH-2 is associated with the cell surfaces of both the signaling, and the responding, blastomeres. Analysis of chimeric embryos that are composed of aph-2(+) and aph-2(-) blastomeres suggests that aph-2(+) function may be provided by either the signaling or responding blastomere.
Goutte
C
C
Division of Basic Sciences and Molecular and Cellular Biology Program, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA. cegoutte@amherst.edu
Hepler
W
W
Mickey
K M
KM
Priess
J R
JR
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001757:Blastomeres; D017173:Caenorhabditis elegans / Q000196:embryology*; D029742:Caenorhabditis elegans Proteins; D018509:DNA, Helminth; D015801:Helminth Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008562:Membrane Glycoproteins / Q000378:metabolism*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D016296:Mutagenesis; D011817:Rabbits; D051880:Receptors, Notch; D015398:Signal Transduction
D029742:Caenorhabditis elegans Proteins; D018509:DNA, Helminth; C060620:Glp-1 protein, C elegans; D015801:Helminth Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D051880:Receptors, Notch; C410543:aph-2 protein, C elegans