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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
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Synaptotagmins interact with APP and promote Aβ generation.

Vivek Gautam1, Carla D'Avanzo2, Oksana Berezovska3

  • 1Genetics and Aging Research Unit, MassGeneral Institute for Neurodegenerative Disease, Massachusetts General Hospital, Harvard Medical School, Charlestown, MA, 02129, USA. gautam.vivek@mgh.harvard.edu.

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Synaptic vesicle proteins Synaptotagmin-1 and -9 interact with amyloid precursor protein (APP) and promote amyloid-beta (Aβ) generation, suggesting a role in Alzheimer

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Alzheimer's disease (AD) is characterized by amyloid-beta (Aβ) peptide accumulation.
  • Synaptic Aβ toxicity impairs neuronal function.
  • Proteins regulating Aβ generation at synapses are largely uncharacterized.

Purpose of the Study:

  • Identify synaptic proteins interacting with the extracellular domain of amyloid precursor protein (APP).
  • Investigate the role of these proteins in regulating Aβ generation.

Main Methods:

  • Affinity purification-coupled mass spectrometry to identify interacting proteins.
  • GST pull-down assays to map interaction sites.
  • Cellular overexpression and knockdown models (CHO, PC12, primary neurons) to assess Aβ generation.
  • Measurement of Aβ, APP-CTF, and sAPP levels.

Main Results:

  • Synaptotagmin (Syt)-1, -2, and -9 identified as novel APP-interacting proteins.
  • Syt interaction site mapped to the APP linker region.
  • Syt-1 and Syt-9 overexpression increased Aβ generation.
  • Syt-1 knockdown significantly reduced Aβ generation in cell lines and primary neurons.
  • Syt-1 regulates Aβ generation by modulating BACE1-mediated APP cleavage.

Conclusions:

  • Synaptic vesicle proteins Syt-1 and Syt-9 are novel APP-interacting proteins.
  • These proteins promote Aβ generation.
  • Syt-1 and Syt-9 may play a significant role in Alzheimer's disease pathogenesis.