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J Biol Chem, Vol. 274, Issue 14, 9141-9148, April 2, 1999
,
From the 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 Max Planck Institute for Experimental
Medicine, 37075 Göttingen, Germany, the ¶ Center for
Molecular Biology, INF 282, 69120 Heidelberg, Germany, and the
Department of Molecular Genetics and the Howard Hughes Medical
Institute, University of Texas, Southwestern Medical Center,
Dallas, Texas 75235
-catenin and APC, are
known to participate in cellular signaling, p0071 may function as a
mediator of presenilin 1 in signaling events.
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