Article
Presenilins mutated at Asp-257 or Asp-385 restore Pen-2 expression and Nicastrin glycosylation but remain catalytically inactive in the absence of wild type Presenilin.
The Journal of biological chemistry - 31 Oct 2003
Nyabi Omar, Bentahir Mostafa, Horré Katrien, Herreman An, Gottardi-Littell Numa, Van Broeckhoven Christine, Merchiers Pascal, Spittaels Kurt, Annaert Wim, De Strooper Bart
Abstract excerpt
The Presenilins are part of the gamma-secretase complex that is involved in the regulated intramembrane proteolysis of amyloid precursor protein and other type I integral membrane proteins. Nicastrin, Pen-2, and Aph1 are the other proteins of this complex. The Presenilins probably contribute the catalytic activity to the protease complex. However, several investigators reported normal Abeta-peptide generation in...
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