Journal article
Phosphorylation of amyloid precursor protein at threonine 668 is essential for its copper-responsive trafficking in SH-SY5Y neuroblastoma cells
KM Acevedo, CM Opazo, D Norrish, LM Challis, QX Li, AR White, AI Bush, J Camakaris
Journal of Biological Chemistry | Published : 2014
Abstract
Background: The function, localization, and processing of the amyloid precursor protein (APP) is regulated by phosphorylation. Results: Copper promotes APP trafficking by phosphorylation at threonine 668 in SH-SY5Y cells. Conclusion: By promoting APP phosphorylation, copper regulates its intracellular localization. Significance: Understanding the role copper plays in regulating APP function in normal neuronal cells will provide insight into the interplay between copper and APP in normal and pathological conditions. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
Grants
Funding Acknowledgements
This work was supported by grants from the National Health and Medical Research Council (to J. C.).