Presenilin 1 is actively degraded by the 26S proteasome

P. E. Fraser, G. Levesque, G. Yu, L. R. Mills, J. Thirlwell, M. Frantseva, S. E. Gandy, M. Seeger, P. L. Carlen, P. St George-Hyslop

Research output: Contribution to journalArticlepeer-review

73 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)S19-S21
JournalNeurobiology of Aging
Issue numberSUPPL. 1
StatePublished - Jan 1998


  • Alzheimer Disease
  • Degradation
  • Endoplasmic reticulum
  • PS1
  • PS2
  • Presenilin
  • Proteasome
  • Proteolysis
  • Transmembrane protein

ASJC Scopus subject areas

  • Neuroscience(all)
  • Aging
  • Clinical Neurology
  • Developmental Biology
  • Geriatrics and Gerontology


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