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

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 protein. Presenilins also facilitate the activity of transmembrane receptors of the LIN-12/Notch fami...

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Bibliographic Details
Published in:Nature (London) 1999-04, Vol.398 (6727), p.522-525
Main Authors: Struhl, Gary, Greenwald, Iva
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Cell Nucleus - metabolism
Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases
Drosophila
Drosophila Proteins
Female
Humanities and Social Sciences
letter
Male
Medical sciences
Membrane Proteins - genetics
Membrane Proteins - metabolism
multidisciplinary
Mutation
Neurology
Presenilins
Receptors, Notch
Science
Science (multidisciplinary)
Signal Transduction
Trans-Activators - genetics
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Summary: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 protein. Presenilins also facilitate the activity of transmembrane receptors of the LIN-12/Notch family. After ligand-induced processing, the intracellular domain of LIN-12/Notch can enter the nucleus and participate in the transcriptional control of downstream target genes. 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.
ISSN:0028-0836
1476-4687
DOI:10.1038/19091