Nov 4, 2017

Recruitment of the amyloid precursor protein by γ-secretase at the synaptic plasma membrane

Biochemical and Biophysical Research Communications
Martina AudagnottoMatteo Dal Peraro


Γ-secretase is a membrane-embedded protease that cleaves single transmembrane helical domains of various integral membrane proteins. The amyloid precursor protein (APP) is an important substrate due to its pathological relevance to Alzheimer's disease. The mechanism of the cleavage of APP by γ-secretase that leads to accumulation of Alzheimer's disease causing amyloid-β (Aβ) is still unknown. Coarse-grained molecular dynamics simulations in this study reveal initial lipids raft formation near the catalytic site of γ-secretase as well as changes in dynamic behavior of γ-secretase once interacting with APP. The results suggest a precursor of the APP binding mode and hint at conformational changes of γ-secretase in the nicastrin (NCT) domain upon APP binding.

  • References
  • Citations1


  • We're still populating references for this paper, please check back later.
  • References
  • Citations1


Mentioned in this Paper

Molecular Dynamics
APP protein, human
Integral Membrane Proteins
Peptide Hydrolases
Amyloid Beta Precursor Protein Measurement
Cytokinesis of the Fertilized Ovum
Integral to Membrane

Related Feeds

Alzheimer's Disease: APP

Amyloid precursor protein proteolysis is critical for the development of Alzheimer's disease, a neurodegenerative disease associated with accumulation of amyloid plaques. Here is the latest research.

Alzheimer's Disease: Abeta

Alzheimer's disease (AD) is a chronic neurodegenerative disease associated with accumulation of amyloid plaques, which are comprised of amyloid beta. Here is the latest research in this field.