Presenilin 1 is actively degraded by the 26S proteasome.
The metabolic pathways governing the turnover of presenilin 1 (PS1) have been incompletely worked out. The PS1 holoprotein has low abundance in many cells and appears to undergo endoproteolytic cleavage near residue 298. We provide evidence that one mechanism by which the PS1 holoprotein is degraded is through the action of the 26S proteasome. We also show that the proteasome does not participate in the endoproteolytic cleavage.
Fraser
P E
PE
Centre for Research in Neurodegenerative Diseases, Department of Medicine, The Toronto Hospital, University of Toronto, Ontario, Canada.
Levesque
G
G
Yu
G
G
Mills
L R
LR
Thirlwell
J
J
Frantseva
M
M
Gandy
S E
SE
Seeger
M
M
Carlen
P L
PL
St George-Hyslop
P
P
D000544:Alzheimer Disease / Q000378:metabolism*; D000818:Animals; D015153:Blotting, Western; D018938:Caco-2 Cells; D006624:Hippocampus / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice; D016328:NF-kappa B / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D053764:Presenilin-1; D046988:Proteasome Endopeptidase Complex; D051381:Rats; D017208:Rats, Wistar
D008565:Membrane Proteins; D016328:NF-kappa B; C508853:PSEN1 protein, human; D053764:Presenilin-1; D010447:Peptide Hydrolases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease