Assembly, Trafficking and Function of γ-Secretase

@article{Kaether2006AssemblyTA,
  title={Assembly, Trafficking and Function of $\gamma$-Secretase},
  author={Christoph Kaether and Christian Haass and Harald Steiner},
  journal={Neurodegenerative Diseases},
  year={2006},
  volume={3},
  pages={275 - 283}
}
γ-Secretase catalyzes the final cleavage of the β-amyloid precursor protein to generate amyloid-β peptide, the principal component of amyloid plaques in the brains of patients suffering from Alzheimer’s disease. Here, we review the identification of γ-secretase as a protease complex and its assembly and trafficking to its site(s) of cellular function. In reconstitution experiments, γ-secretase was found to be composed of four integral membrane proteins, presenilin (PS), nicastrin (NCT), PEN-2… 
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Endoplasmic reticulum retention of the γ‐secretase complex component Pen2 by Rer1
TLDR
Retention in endoplasmic reticulum 1 (Rer1) is identified as a protein that is involved in the retention/retrieval of unassembled Pen2 to the ER and Rer1 is the first identified interaction partner of mammalian transmembrane‐based retention/ retrieval signals.
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TLDR
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TLDR
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TLDR
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