A CBP Binding Transcriptional Repressor Produced by the PS1/ϵ-Cleavage of N-Cadherin Is Inhibited by PS1 FAD Mutations
@article{Marambaud2003ACB, title={A CBP Binding Transcriptional Repressor Produced by the PS1/ϵ-Cleavage of N-Cadherin Is Inhibited by PS1 FAD Mutations}, author={Philippe Marambaud and Paul H. Wen and Anindita Dutt and Jun-ichi Shioi and Akihiko Takashima and Robert G. Siman and Nikolaos K. Robakis}, journal={Cell}, year={2003}, volume={114}, pages={635-645} }
446 Citations
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Characterization of sequential N-cadherin cleavage by ADAM10 and PS1
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Activity-dependent regulation of beta-catenin via epsilon-cleavage of N-cadherin.
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Gamma-Secretase-Dependent and -Independent Effects of Presenilin1 on β-Catenin·Tcf-4 Transcriptional Activity
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It is shown that in murine embryonic fibroblasts (MEFs) the mechanisms of action of the processed and non-processed forms of PS1 on β-catenin·Tcf-4 transcription are different, indicating that prevention of PS 1 processing in FAD affects the mechanism of repression of the transcriptional activity dependent onβ- catenin.
Presenilin-Dependent Transcriptional Control of the Aβ-Degrading Enzyme Neprilysin by Intracellular Domains of βAPP and APLP
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The product of the γ-secretase processing of ephrinB2 regulates VE-cadherin complexes and angiogenesis
- Biology, ChemistryCellular and Molecular Life Sciences
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Evidence is presented that the cytosolic peptide efnB2/CTF2 produced by the PS1/γ-secretase cleavage of efn B2 ligand promotes EphB4 receptor-dependent angiogenesis in vitro.
GSK3β Activity Modifies the Localization and Function of Presenilin 1*
- Biology, ChemistryJournal of Biological Chemistry
- 2007
The findings indicate that the abnormal activation of glycogen synthase kinase 3β can reduce neuronal viability and synaptic plasticity via modulating Presenilin 1/N-cadherin/β-catenin interaction and thus have important implications in the pathophysiology of Alzheimer disease.
A Role for the Cleaved Cytoplasmic Domain of E-cadherin in the Nucleus*S⃞
- BiologyJournal of Biological Chemistry
- 2008
It is shown that coexpression of the cadherin-binding protein, p120 catenin (p120), enhances the nuclear translocation of E-cad/CTF2 and can regulate the p120-Kaiso-mediated signaling pathway in the nucleus.
p120 Catenin Recruits Cadherins to γ-Secretase and Inhibits Production of Aβ Peptide*
- BiologyJournal of Biological Chemistry
- 2009
It is reported that p120 catenin (p120ctn), a component of the cadherin-catenin complex, recruits γ-secretase to cadherins, thus stimulating their processing while inhibiting production of Aβ peptide and the amyloid precursor protein intracellular domain.
Cadherins Mediate Both the Association between PS1 and β-Catenin and the Effects of PS1 on β-Catenin Stability*
- Biology, ChemistryJournal of Biological Chemistry
- 2005
It is shown that binding of PS1 to cadherin mediates the effects ofPS1 on the phosphorylation, ubiquitination, and destabilization of β-catenin.
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