Presenilin mutations associated with Alzheimer disease cause defective intracellular trafficking of β-catenin,a component of the presenilin protein complex View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-02

AUTHORS

M. Nishimura, G. Yu, G. Levesque, D.M. Zhang, L. Ruel, F. Chen, P. Milman, E. Holmes, Y. Liang, T. Kawarai, E. Jo, A. Supala, E. Rogaeva, D -M. Xu, C. Janus, L. Levesque, Q. Bi, M. Duthie, R. Rozmahel, K. Mattila, L. Lannfelt, D. Westaway, H.T.J. Mount, J. Woodgett, P.E. Fraser, P. St George–Hyslop

ABSTRACT

The presenilin proteins are components of high–molecular–weight protein complexes in the endoplasmic reticulum and Golgi apparatus that also contain β-catenin. We report here that presenilin mutations associated with familial Alzheimer disease (but not the non–pathogenic Glu318Gly polymorphism) alter the intracellular trafficking of β-catenin after activation of the Wnt/β-catenin signal transduction pathway. As with their effect on βAPP processing, the effect of PS1 mutations on trafficking of β-catenin arises from a dominant 'gain of aberrant function' activity. These results indicate that mistrafficking of selected presenilin ligands is a candidate mechanism for the genesis of Alzheimer disease associated with presenilin mutations, and that dysfunction in the presenilin–β-catenin protein complexes is central to this process. More... »

PAGES

164-169

Journal

TITLE

Nature Medicine

ISSUE

2

VOLUME

5

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/5526

    DOI

    http://dx.doi.org/10.1038/5526

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1036650705

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9930863


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