aph-2 encodes a novel extracellular protein required for GLP-1-mediated signaling

Development. 2000 Jun;127(11):2481-92. doi: 10.1242/dev.127.11.2481.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blastomeres
  • Caenorhabditis elegans / embryology*
  • Caenorhabditis elegans Proteins*
  • DNA, Helminth
  • Helminth Proteins / genetics
  • Helminth Proteins / metabolism*
  • Humans
  • Membrane Glycoproteins / metabolism*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Mutagenesis
  • Rabbits
  • Receptors, Notch
  • Signal Transduction*

Substances

  • Caenorhabditis elegans Proteins
  • DNA, Helminth
  • Glp-1 protein, C elegans
  • Helminth Proteins
  • Membrane Glycoproteins
  • Membrane Proteins
  • Receptors, Notch
  • aph-2 protein, C elegans