APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos
| Autor: | Makoto Tsunozaki, Caroline Goutte, Valerie A. Hale, James R Priess |
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| Rok vydání: | 2002 |
| Předmět: |
Molecular Sequence Data
Notch signaling pathway Nicastrin Presenilin PEN-2 Animals Amino Acid Sequence APH-1 Caenorhabditis elegans Caenorhabditis elegans Proteins Genes Helminth Homeodomain Proteins Membrane Glycoproteins Multidisciplinary Receptors Notch Sequence Homology Amino Acid biology Cell Membrane Membrane Proteins Helminth Proteins Biological Sciences biology.organism_classification Cell biology Gamma-secretase complex Phenotype Membrane protein Mutation biology.protein Amyloid Precursor Protein Secretases Signal Transduction |
| Zdroj: | Proceedings of the National Academy of Sciences. 99:775-779 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.022523499 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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