Dual roles of the transmembrane protein p23/TMP21 in the modulation of amyloid precursor protein metabolism.

ABSTRACT:

Background

Alzheimer's disease (AD) is characterized by cerebral deposition of beta-amyloid (Abeta) peptides. Abeta is released from ectodomain cleaved amyloid precursor protein (APP) via intramembranous proteolysis by gamma-secretase, a complex consisting of presenilin and a few other proteins. p23/TMP21, a member of the p24 family type I transmembrane proteins, was recently identified as a presenilin complex component capable of modulating gamma-secretase cleavage. The p24 family proteins form oligomeric complexes and regulate vesicular trafficking in the early secretory pathway, but their role in APP trafficking has not been investigated.

Results

Here, we report that siRNA-mediated depletion of p23 in N2a neuroblastoma and HeLa cells produces concomitant knockdown of addi

SUBMITTER: Vetrivel KS 

PROVIDER: S-EPMC1803014 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature