Abstract
Early embryonic cells in Caenorhabditis elegans embryos interact through a signaling pathway closely related to the Notch signaling pathway in Drosophila and vertebrates. Components of this pathway include a ligand, receptor, the presenilin proteins, and a novel protein, APH-2, that is related to the Nicastrin protein in humans. Here we identify the aph-1 gene as a new component of the Notch pathway in Caenorhabditis elegans. aph-1 is predicted to encode a novel, highly conserved multipass membrane protein. We show that aph-1 and the presenilin genes share a similar function in that they are both required for proper cell-surface localization of APH-2/Nicastrin.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Amyloid Precursor Protein Secretases
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Animals
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Caenorhabditis elegans / embryology*
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Caenorhabditis elegans / genetics*
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Caenorhabditis elegans Proteins / genetics*
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Caenorhabditis elegans Proteins / physiology*
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Cell Membrane / physiology
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Genes, Helminth
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Helminth Proteins / genetics
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Helminth Proteins / physiology
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Homeodomain Proteins / genetics*
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Homeodomain Proteins / physiology*
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / physiology
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Membrane Proteins / genetics*
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Membrane Proteins / physiology*
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Molecular Sequence Data
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Mutation
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Phenotype
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Receptors, Notch
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Sequence Homology, Amino Acid
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Signal Transduction
Substances
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APH-1 protein, C elegans
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Caenorhabditis elegans Proteins
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Helminth Proteins
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Homeodomain Proteins
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Membrane Glycoproteins
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Membrane Proteins
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Receptors, Notch
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aph-2 protein, C elegans
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nicastrin protein
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Amyloid Precursor Protein Secretases