Microtubular interactions of presenilin direct kinesis of Abeta peptide and its precursors.

In our previous study we demonstrated that presenilin 1 (PS1) interacts with cytoplasmic linker protein 170/Restin (CLIP-170/Restin). Herein we show that disruption of the interaction of these proteins within neuronal cell-lines (SY5Y and N2a) can be accomplished by the transfection of vectors that drive the expression of peptide fragments corresponding to their binding domains (BDPs). Interestingly, the disruption of the PS1/CLIP-170 complex is associated with both decreased secretion of endogenous Abeta and decreased uptake of exogenous Abeta from the medium.