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• W2790085711 abstract "Presenilin 1 (PS1) is a component of the -secretase complex that cleaves a variety of type I mem- brane proteins, including the -amyloid precursor protein (-APP), Notch, and neuronal (N)- and epithelial (E)- cadherins. N-cadherin is an essential adhesion molecule that forms a complex with, and is cleaved by, PS1/- secretase and -catenin in the plasma membrane. The purpose of this study was to determine whether calsenilin, a presenilin-interacting protein, has a functional role in PS1/-secretase-mediated N-cadherin -cleavage using Western blot analysis, RT-PCR, immunoprecipitation, subcellular fractionation, biotinylation, and a luciferase reporter assay in SH-SY5Y neuroblastoma cells. Here, we demonstrate that the expression of calsenilin leads to a disruption of PS1/-secretase-mediated -cleavage of N- cadherin, which results in the significant accumulation of N-cadherin C-terminal fragment 1 (Ncad/CTF1), the re- duction of cytoplasmic Ncad/CTF2 release, and a decel- eration of PS1-CTF delivery to the cell surface. Interest- ingly, we also found that the expression of calsenilin is associated with the redistribution of -catenin from the cell surface to a cytoplasmic pool, as well as with the negative regulation of genes that are targets of T-cell factor/-catenin nuclear signaling. Taken together, our findings suggest that calsenilin is a novel negative regula- tor of N-cadherin processing that plays an important role in -catenin signaling.—Jang, C., Choi, J.-K., Na, Y.-J., Jang, B., Wasco, W., Buxbaum, J. D., Kim, Y.-S., Choi, E.-K. Calsenilin regulates presenilin 1/-secretase-medi- ated N-cadherin -cleavage and -catenin signaling. FASEB J. 25, 000-000 (2011). www.fasebj.org" @default.
• W2790085711 created "2018-03-29" @default.
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• W2790085711 date "2011-01-01" @default.
• W2790085711 modified "2023-09-26" @default.
• W2790085711 title "Calsenilin regulates presenilin 1/-secretase-mediated N-cadherin -cleavage and -catenin signaling" @default.
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