JBC Transcription and Nuclear Factor Monoclonals

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J Biol Chem, Vol. 273, Issue 51, 33909-33914, December 18, 1998

Abrogation of the Presenilin 1/beta -Catenin Interaction and Preservation of the Heterodimeric Presenilin 1 Complex following Caspase Activation

Giuseppina Tesco, Tae-Wan Kim, Anke Diehlmann, Konrad Beyreuther, and Rudolph E. Tanzi

From the Genetics and Aging Unit, Massachusetts General Hospital and Harvard Medical School, Charlestown, Massachusetts 02129 and the  Zentrum für Molekulare Biologie Heidelberg, INF 282, 69120 Heidelberg, Federal Republic of Germany

beta -Catenin has previously been shown to interact with presenilin 1 (PS1) in transfected cells. Here we report that beta -catenin co-immunoprecipitates with the endogenous C-terminal fragment of presenilin 1 (PS1-CTF) but not with the endogenous CTF of presenilin 2 (PS2-CTF) in H4 human neuroglioma cells. During staurosporine (STS)-induced cell death, beta -catenin and PS1-CTF undergo a caspase-mediated cleavage. After 12 h of STS treatment, the beta -catenin·PS1-CTF interaction is abrogated. While PS1-CTF immunoprecipitated with all caspase-cleaved species of beta -catenin, beta -catenin holoprotein did not co-immunoprecipitate with the "alternative" caspase-derived PS1-CTF (PS1-aCTF). Thus, the abrogation of the beta -catenin·PS1-CTF complex was due to caspase cleavage of PS1-CTF. beta -Catenin co-immunoprecipitated with PS1-NTF, but only when PS1-NTF was associated with PS1-CTF. Even though PS1-NTF·CTF complex stability was not altered by caspase cleavage, its ability to bind beta -catenin was abolished. Thus, while the PS1-NTF·CTF complex is preserved after caspase cleavage, it may no longer be fully functional.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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