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Nuclear localization of amyloid-beta precursor protein-binding protein Fe65 is dependent on regulated intramembrane proteolysis
Stockholm University, Faculty of Science, Department of Neurochemistry.
Stockholm University, Faculty of Science, Department of Neurochemistry.
Stockholm University, Faculty of Science, Department of Neurochemistry.
Stockholm University, Faculty of Science, Department of Neurochemistry.
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Number of Authors: 6
2017 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 12, no 3, 1-14 p., e0173888Article in journal (Refereed) Published
Abstract [en]

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 theWWdomain 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.

Place, publisher, year, edition, pages
2017. Vol. 12, no 3, 1-14 p., e0173888
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-143465DOI: 10.1371/journal.pone.0173888ISI: 000399089000040PubMedID: 28323844OAI: oai:DiVA.org:su-143465DiVA: diva2:1104984
Available from: 2017-06-02 Created: 2017-06-02 Last updated: 2017-06-02Bibliographically approved

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Koistinen, Niina A.Edlund, Anna K.Menon, Preeti K.Ivanova, Elena V.Iverfeldt, Kerstin
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