Nuclear localization of amyloid- square precursor protein-binding protein Fe65 is dependent on regulated intramembrane proteolysis

Fe65 is an adaptor protein involved in both processing and signaling of the Alzheimer-associated amyloid-[Beta] precursor protein, APP. Here, the subcellular localization was further investigated using TAP-tagged Fe65 constructs expressed in human neuroblastoma cells. Our results indicate that PTB2...

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Bibliographic Details
Published in:PloS one 2017-03, Vol.12 (3)
Main Authors: Koistinen, Niina A, Edlund, Anna K, Menon, Preeti K, Ivanova, Elena V, Bacanu, Smaranda, Iverfeldt, Kerstin
Format: Article
Language:English
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Summary:Fe65 is an adaptor protein involved in both processing and signaling of the Alzheimer-associated amyloid-[Beta] precursor protein, APP. Here, the subcellular localization was further investigated using TAP-tagged Fe65 constructs expressed in human neuroblastoma cells. Our results indicate that PTB2 rather than the WW domain is important for the nuclear localization of Fe65. Electrophoretic mobility shift of Fe65 caused by phosphorylation was not detected in the nuclear fraction, suggesting that phosphorylation could restrict nuclear localization of Fe65. Furthermore, both ADAM10 and gamma -secretase inhibitors decreased nuclear Fe65 in a similar way indicating an important role also of alpha -secretase in regulating nuclear translocation.
ISSN:1932-6203
DOI:10.1371/journal.pone.0173888