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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Gamma-secretase activity is not involved in presenilin- mediated regulation of beta-catenin.

Presenilins (PS) are involved in gamma-secretase-mediated processing of beta-amyloid precursor protein (APP) and the Notch family of proteins. In addition, presenilin 1 (PS-1) binds to members of the armadillo family of proteins. In this study the relationship between PS-1- mediated proteolytic activity and PS-1- mediated regulation of beta-catenin function was investigated. Incubation of cells with a potent, small molecule gamma-secretase inhibitor did not affect PS-1/beta-catenin interaction as determined by co-immunoprecipitation, or affect the regulation of beta-catenin turnover, as determined by pulse-chase analysis, even at inhibitor concentrations that completely blocked PS-mediated APP processing. Moreover, inhibition of PS-1- mediated proteolytic activity did not affect beta-catenin trafficking, as determined by immunolocalization and immunoblotting, or beta-catenin-mediated transcription. These results indicate that PS-1- mediated regulation of gamma-secretase activity and PS-1- mediated regulation of beta-catenin function can be pharmacologically separated and support the idea that these are distinct functions.[1]

References

  1. Gamma-secretase activity is not involved in presenilin-mediated regulation of beta-catenin. Meredith, J.E., Wang, Q., Mitchell, T.J., Olson, R.E., Zaczek, R., Stern, A.M., Seiffert, D. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
 
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