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.

References

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. Abstract

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. Abstract