PRESENILIN-1 IS ACTIVELY DEGRADED BY THE 26S PROTEASOME

Authors
FRASER PE LEVESQUE G YU G MILLS LR THIRLWELL J FRANTSEVA M GANDY SE SEEGER M CARLEN PL GEORGEHYSLOP PS
Citation
Pe. Fraser et al., PRESENILIN-1 IS ACTIVELY DEGRADED BY THE 26S PROTEASOME, Neurobiology of aging, 19(1), 1998, pp. 19-21
Citations number
18
Categorie Soggetti
Neurosciences,"Geiatric & Gerontology
Journal title
Neurobiology of aging → ACNP
ISSN journal
01974580
Volume
19
Issue
1
Year of publication
1998
Supplement
1
Pages
19 - 21
Database
ISI
SICI code
0197-4580(1998)19:1<19:PIADBT>2.0.ZU;2-I
Abstract
The metabolic pathways governing the turnover of presenilin 1 (PS I) h ave been incompletely worked out. The PS 1 holoprotein has low abundan ce in many cells and appears to undergo endoproteolytic cleavage near residue 298. We provide evidence that one mechanism by which the PSI h oloprotein is degraded is through the action of the 26S proteasome. We also show that the proteasome does not participate in the endoproteol ytic cleavage. (C) 1998 Elsevier Science Inc.