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Updated: Apr 14, 2026
Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
Published on: October 17, 2015
PAT1 inversely regulates the surface Amyloid Precursor Protein level in mouse primary neurons
Aysegul Dilsizoglu Senol1, Lidia Tagliafierro2, Léa Huguet3
1INSERM UMR 894, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Médecine, Paris, France. aysdilsizoglu@yahoo.com.
Background:
The amyloid precursor protein (APP) is a key molecule in Alzheimer disease. Its localization at the cell surface can trigger downstream signaling and APP cleavages. APP trafficking to the cell surface in neurons is not clearly understood and may be related to the interactions with its partners. In this respect, by having homologies with kinesin light chain domains and because of its capacity to bind APP, PAT1 represents a good candidate.
Results:
We observed that PAT1 binds poorly APP at the cell surface of primary cortical neurons contrary to cytoplasmic APP. Using down and up-regulation of PAT1, we observed respectively an increase and decrease of APP at the cell surface. The increase of APP at the cell surface induced by low levels of PAT1 did not trigger cell death signaling.
Conclusions:
These data suggest that PAT1 slows down APP trafficking to the cell surface in primary cortical neurons. Our results contribute to the elucidation of mechanisms involved in APP trafficking in Alzheimer disease.
