Title: Cellular localization of Nicastrin affects amyloid beta species production
Authors: Morais, Vanessa
Leight, Susan
Pijak, Donald S
Lee, Virginia M. -Y
Costa, Julia # ×
Issue Date: Feb-2008
Publisher: Elsevier on behalf of the Federation of European Biochemical Societies
Series Title: FEBS Letters vol:582 issue:3 pages:427-433
Abstract: The gamma-secretase complex, composed by presenilin, nicastrin, APH-1 and PEN-2, is involved in intramembranous proteolysis of membrane proteins, such as amyloid precursor protein or Notch. Cleavage occurs in multiple cellular compartments. Here, nicastrin mutants containing targeting signals to the endoplasmic reticulum, trans-Golgi network, lysosomes, or plasma membrane have been shown to yield active gamma-secretase complexes with different activities and specificities: wild-type and plasma membrane nicastrin complexes yielded the highest amounts of secreted amyloid-beta peptide (A beta), predominantly A beta 40, whereas intracellular targeted mutants produced intracellular A beta, with a comparatively higher amount of A beta 42. These results suggest that compartmental microenvironments play a role in gamma-secretase activity and specificity. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
ISSN: 0014-5793
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory for the Research of Neurodegenerative Diseases
× corresponding author
# (joint) last author

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