• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


Direct interaction of Alzheimer's disease-related presenilin 1 with armadillo protein p0071.

Alzheimer's disease-related presenilins are thought to be involved in Notch signaling during embryonic development and/or cellular differentiation. Proteins mediating the cellular functions of the presenilins are still unknown. We utilized the yeast two-hybrid system to identify an interacting armadillo protein, termed p0071, that binds specifically to the hydrophilic loop of presenilin 1. In vivo, the presenilins constitutively undergo proteolytic processing, forming two stable fragments. Here, we show that the C-terminal fragment of presenilin 1 directly binds to p0071. Nine out of 10 armadillo repeats in p0071 are essential for mediating this interaction. Since armadillo proteins, like beta-catenin and APC, are known to participate in cellular signaling, p0071 may function as a mediator of presenilin 1 in signaling events.

Pubmed ID: 10092585


  • Stahl B
  • Diehlmann A
  • S├╝dhof TC


The Journal of biological chemistry

Publication Data

April 2, 1999

Associated Grants


Mesh Terms

  • Alzheimer Disease
  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Cloning, Molecular
  • Cytoskeletal Proteins
  • Humans
  • Membrane Proteins
  • Mice
  • Molecular Sequence Data
  • Plakophilins
  • Presenilin-1
  • Presenilin-2
  • Protein Binding
  • Rats
  • Signal Transduction
  • Trans-Activators
  • Transfection
  • beta Catenin