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Presenilin is required for activity and nuclear access of Notch in Drosophila

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Listed:
  • Gary Struhl

    (Departments of Genetics and Development
    Columbia University, College of Physicians and Surgeons)

  • Iva Greenwald

    (Columbia University, College of Physicians and Surgeons
    Departments of Biochemistry and Molecular Biophysics)

Abstract

Presenilins are membrane proteins with multiple transmembrane domains that are thought to contribute to the development of Alzheimer's disease by affecting the processing of β-amyloid precursor protein1. Presenilins also facilitate the activity of transmembrane receptors of the LIN-12/Notch family2,3,4,5. After ligand-induced processing, the intracellular domain of LIN-12/Notch can enter the nucleus and participate in the transcriptional control of downstream target genes6,7,8,9. Here we show that null mutations in the Drosophila Presenilin gene abolish Notch signal transduction and prevent its intracellular domain from entering the nucleus. Furthermore, we provide evidence that presenilin is required for the proteolytic release of the intracellular domain from the membrane following activation of Notch by ligand.

Suggested Citation

  • Gary Struhl & Iva Greenwald, 1999. "Presenilin is required for activity and nuclear access of Notch in Drosophila," Nature, Nature, vol. 398(6727), pages 522-525, April.
    • Handle: RePEc:nat:nature:v:398:y:1999:i:6727:d:10.1038_19091
    DOI: 10.1038/19091
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    Cited by:

    1. Anika Perdok & Zoë P. Van Acker & Céline Vrancx & Ragna Sannerud & Inge Vorsters & Assunta Verrengia & Zsuzsanna Callaerts-Végh & Eline Creemers & Sara Gutiérrez Fernández & Britt D’hauw & Lutgarde Se, 2024. "Altered expression of Presenilin2 impacts endolysosomal homeostasis and synapse function in Alzheimer’s disease-relevant brain circuits," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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