APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos
Open Access
- 15 January 2002
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 99 (2) , 775-779
- https://doi.org/10.1073/pnas.022523499
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.Keywords
This publication has 38 references indexed in Scilit:
- Notch Signaling: Cell Fate Control and Signal Integration in DevelopmentScience, 1999
- THE LIN-12/Notch SIGNALING PATHWAY AND ITS REGULATIONAnnual Review of Cell and Developmental Biology, 1997
- Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease geneNature, 1995
- Translational control of maternal glp-1 mRNA establishes an asymmetry in the C. elegans embryoCell, 1994
- The maternal genes apx-1 and glp-1 and establishment of dorsal-ventral polarity in the early C. elegans embryoCell, 1994
- An Organ-Specific Differentiation Gene, pha-1 , from Caenorhabditis elegansScience, 1990
- The glp-1 locus and cellular interactions in early C. elegans embryosCell, 1987
- glp-1 Is required in the germ line for regulation of the decision between mitosis and meiosis in C. elegansCell, 1987
- Cellular interactions in early C. elegans embryosCell, 1987
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982