Assembly of the presenilin γ-/ε-secretase complex

J Neurochem. 2012 Jan:120 Suppl 1:84-88. doi: 10.1111/j.1471-4159.2011.07505.x. Epub 2011 Nov 28.

Abstract

The presenilin complex is composed of four core proteins (presenilin 1 or presenilin 2, APH1, nicastrin, and PEN2). Several endogenous proteins have been reported to selectively modulate the function of the presenilin complexes; these include transmembrane trafficking protein, 21-KD (TMP21), CD147 antigen (basigin), the γ-secretase-activating protein (gSAP), and the orphan G-protein-coupled receptor 3. Because the structure and assembly of these complexes underlies their activity, this review will discuss current work on the assembly of the complex and on presenilin-interacting proteins that regulate secretase activity.

Publication types

  • Review

MeSH terms

  • Alzheimer Disease / enzymology*
  • Alzheimer Disease / metabolism
  • Amyloid Precursor Protein Secretases / chemistry
  • Amyloid Precursor Protein Secretases / metabolism*
  • Amyloid Precursor Protein Secretases / physiology
  • Amyloid beta-Peptides / chemistry
  • Amyloid beta-Peptides / metabolism
  • Animals
  • Endopeptidases
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / physiology
  • Peptide Hydrolases / chemistry
  • Peptide Hydrolases / physiology
  • Presenilin-1 / chemistry*
  • Presenilin-1 / physiology
  • Presenilin-2 / chemistry*
  • Presenilin-2 / physiology

Substances

  • Amyloid beta-Peptides
  • Membrane Proteins
  • PSEN1 protein, human
  • PSENEN protein, human
  • Presenilin-1
  • Presenilin-2
  • APH1A protein, human
  • Amyloid Precursor Protein Secretases
  • Endopeptidases
  • Peptide Hydrolases