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Updated 12 January 2007
Reprinted from International Review of Cytology, Vol 254, Dillen K. & Annaert W.,
A two decade contribution of molecular cell biology to the centennial of Alzheimer’s
disease: are we progressing towards therapy?, Pages 215-300, Copyright (2006), with
permission from Elsevier
Amino acid representation (numbering of human PSEN1) of the 9-TMD topology of PSEN1,
including exon boundaries. FAD-linked mutations are indicated in red, while non-pathogenic
mutations are marked in orange. Interaction domains with APP/TLN or NCT/APH-1/PEN-2
are marked in blue, as well as the conserved residues D257 and D385 forming the
putative catalytic site. Interactions of the C-terminal domain and the hydrophilic
loop domain with proteins such as the brain G-protein Go, calsenilin, the PSEN1-associated
protein (PSAP), b- and d-catenin, p0071 and PLD1, are shown in dark green. The endoproteolytic
cleavage site separating PSEN1-NTF and -CTF in the seventh hydrophobic region, the
SPP cleavage site in the ninth TMD and the caspase cleavage site in the hydrophilic
loop domain, are indicated by yellow arrows.
Dillen K, Annaert W. A two decade contribution of molecular cell biology to the
centennial of Alzheimer's disease: are we progressing toward therapy? Int Rev Cytol.
2006 ; 254():215-300.
Spasic D, Tolia A, Dillen K, Baert V, De Strooper B, Vrijens S, Annaert W. Presenilin-1
maintains a nine-transmembrane topology throughout the secretory pathway. J Biol
Chem. 2006 Sep 8 ; 281(36):26569-77.