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

Abstract

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
Pages (from-to)S19-S21
JournalNeurobiology of Aging
Volume19
Issue numberSUPPL. 1
DOIs
StatePublished - Jan 1998
Externally publishedYes

Keywords

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

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