A conserved GXXXG motif in APH-1 is critical for assembly and activity of the gamma-secretase complex.

@article{Lee2004ACG,
  title={A conserved GXXXG motif in APH-1 is critical for assembly and activity of the gamma-secretase complex.},
  author={S J Lee and Sanjiv Shah and Cong Yu and W. Christian Wigley and Harry H. Li and Myungsil Lim and Kia Pedersen and Weiping Han and Philip Thomas and Johan Lundkvist and Y Hao and Gang Yu},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 6},
  pages={4144-52}
}
The multipass membrane protein APH-1, found in the gamma-secretase complex together with presenilin, nicastrin, and PEN-2, is essential for Notch signaling in Caenorhabditis elegans embryos and is required for intramembrane proteolysis of Notch and beta-amyloid precursor protein in mammalian and Drosophila cells. In C. elegans, a mutation of the conserved transmembrane Gly123 in APH-1 (mutant or28) leads to a notch/glp-1 loss-of-function phenotype. In this study, we show that the corresponding… CONTINUE READING
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