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Abnormal phosphorylation of amyloid precursor protein tyrosine residues alters the APP trafficking in neurons from Alzheimer's Disease affected patients

Associate Prof Carmela Matrone (Aarhus University, Denmark) presented at the 13th international conference on Alzheimer's & Parkinson's Diseases (ADPD 2017) in Vienna, Austria. During this presentation Prof Matrone used our Human iPSC-Derived Neurons carrying Alzheimer's Disease-associated mutations in presenilin 1 (PSEN1; L286V, A246E, M146L) and controls to demonstrate the following:

Amyloid precursor protein tyrosine residue phosphorylation and the affect this has on:
  • APP binding to clathrin and AP2
  • APP trafficking and sorting 
  • Suggesting that APP tyrosine phosphorylation might be a new valuable target for Alzheimer's Disease.

    Find out more:

    Poulsen ET, Iannuzzi F, Rasmussen HF, et al.An aberrant phosphorylation of amyloid precursor protein tyrosine regulates its trafficking and the binding to the clathrin endocytic complex in neural stem cells of Alzheimer's disease patients. Journal of Frontiers in Molecular Neuroscience (2017)

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