title: APH-2/nicastrin functions in LIN-12/Notch signaling in the Caenorhabditis elegans somatic gonad.
abstract: Nicastrin is a recently identified member of high-molecular weight complexes containing presenilin. The Caenorhabditis elegans homolog of nicastrin, aph-2, was shown to be required for GLP-1/Notch signaling in the early embryo. In addition to the maternal-effect embryonic lethal phenotype, aph-2 mutant animals also display an egg-laying defect. We show that this latter defect is related to the SEL-12/presenilin egg-laying defect. We also show that aph-2 and sel-12 genetically interact and cooperate to regulate LIN-12/Notch signaling in the development of the somatic gonad. In addition, aph-2 and lin-12/Notch genetically interact. We illustrate a new role for aph-2 in facilitating lin-12 signaling in the somatic gonad, thus providing evidence that APH-2 is involved in both GLP-1/Notch- and LIN-12/Notch-mediated signaling events. Finally, we demonstrate that nicastrin can partially substitute for aph-2, suggesting a conservation of function between these proteins.
authors.affiliation: Schering-Plough Research Institute, 2015 Galloping Hill Road, Kenilworth, New Jersey 07033, USA. diane.levitan@spcorp.com
authors.forename: D
authors.initials: D
authors.lastname: Levitan
authors.forename: G
authors.initials: G
authors.lastname: Yu
authors.forename: P
authors.initials: P
authors.lastname: St  George Hyslop
authors.forename: C
authors.initials: C
authors.lastname: Goutte
mesh_terms: D053829:Amyloid Precursor Protein Secretases; D000818:Animals; D030801:Animals, Genetically Modified; D017173:Caenorhabditis elegans / Q000235:genetics* / Q000254:growth & development / Q000502:physiology*; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000502:physiology; D005260:Female; D018507:Gene Expression Regulation, Developmental; D017238:Genes, Helminth; D005836:Genitalia, Female / Q000254:growth & development; D015801:Helminth Proteins / Q000235:genetics* / Q000502:physiology*; D006801:Humans; D008562:Membrane Glycoproteins / Q000235:genetics* / Q000502:physiology*; D008565:Membrane Proteins / Q000235:genetics* / Q000502:physiology*; D009154:Mutation; D010058:Oviposition / Q000235:genetics / Q000502:physiology; D010641:Phenotype; D051880:Receptors, Notch; D015398:Signal Transduction
chemical_list: D029742:Caenorhabditis elegans Proteins; D015801:Helminth Proteins; C082460:Lin-12 protein, C elegans; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D051880:Receptors, Notch; C095907:SEL-12 protein, C elegans; C410543:aph-2 protein, C elegans; C413604:nicastrin protein; D053829:Amyloid Precursor Protein Secretases