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}
}
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References

SHOWING 1-10 OF 91 REFERENCES
Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex
Here we show that presenilin-1 (PS1), a protein involved in Alzheimer's disease, binds directly to epithelial cadherin (E-cadherin). This binding is mediated by the large cytoplasmic loop of PS1 and…
A Dominant-Negative Inhibitor of CREB Reveals that It Is a General Mediator of Stimulus-Dependent Transcription of c-fos
TLDR
The results suggest that CREB or its closely related family members are general mediators of stimulus-dependent transcription of c-fos and are required for at least some of the long-term actions of NGF.
Loss of presenilin 1 is associated with enhanced β-catenin signaling and skin tumorigenesis
TLDR
It is reported here that PS1 is important in controlling epidermal cell proliferation in vivo and that deregulation of β-catenin pathway contributes to the skin tumor phenotype.
Nuclear protein CBP is a coactivator for the transcription factor CREB
TLDR
Fluorescence anisotropy measurements are used to define the equi-librium binding parameters of the phosphoCREB:CBP interaction and report here that CBP can activate transcription through a region in its carboxy terminus.
A presenilin‐1/γ‐secretase cleavage releases the E‐cadherin intracellular domain and regulates disassembly of adherens junctions
TLDR
It is shown that presenilin‐1 (PS1), a protein involved in Alzheimer's disease, controls a γ‐secretase‐like cleavage of E‐cadherin that stimulates disassembly of the E‐ cadher in– catenin complex and increases the cytosolic pool of β‐catenin, a key regulator of the Wnt signaling pathway.
Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1
Cleavage of amyloid precursor protein (APP) by the β- and γ-secretases generates the amino and carboxy termini, respectively, of the Aβ amyloidogenic peptides Aβ40 and Aβ42—the major constituents of…
Activation of cAMP and mitogen responsive genes relies on a common nuclear factor
TLDR
It is reported here that micro-injection of an anti-CBP antiserum into fibroblasts can inhibit transcription from a cAMP responsive promoter, and proposed that CBP is recruited to the promoter through interaction with certain phosphorylated factors, and may thus play a critical role in the transmission of inductive signals from cell surface receptor to the transcriptional apparatus.
CBP/p300 in cell growth, transformation, and development.
TLDR
This review focuses on the involvement of CBP/p300 in the complex biological processes that affect cell growth, transformation, and development.
Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
TLDR
The results indicate that mutations in PS1 that manifest clinically cause a gain of function and that inhibition of PS1 activity is a potential target for anti-amyloidogenic therapy in Alzheimer's disease.
Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
TLDR
The results indicate that the two transmembrane aspartate residues are critical for both presenilin-1 endoproteolysis and γ-secretase activity, and suggest that presenILin 1 is either a unique diaspartyl cofactor for ιsecretase or is itselfγ- secretase, an autoactivated intramembranous aspartyl protease.
...
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