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Your search keyword '"Elena V. Ivanova"' showing total 2 results
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2 results on '"Elena V. Ivanova"'

1. Nuclear localization of amyloid-β precursor protein-binding protein Fe65 is dependent on regulated intramembrane proteolysis

Author

Niina A Koistinen, Anna K Edlund, Preeti K Menon, Elena V Ivanova, Smaranda Bacanu, and Kerstin Iverfeldt

Subjects
lcsh:R, lcsh:Medicine, lcsh:Q, lcsh:Science
Abstract

Fe65 is an adaptor protein involved in both processing and signaling of the Alzheimer-associated amyloid-β 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 γ-secretase inhibitors decreased nuclear Fe65 in a similar way indicating an important role also of α-secretase in regulating nuclear translocation.

Published
2017

2. Nuclear localization of amyloid-β precursor protein-binding protein Fe65 is dependent on regulated intramembrane proteolysis

Author

Niina A, Koistinen, Anna K, Edlund, Preeti K, Menon, Elena V, Ivanova, Smaranda, Bacanu, and Kerstin, Iverfeldt

Subjects
Cytoplasm, Subcellular Fractionation, Recombinant Fusion Proteins, Mutagenesis and Gene Deletion Techniques, Cell Membranes, Active Transport, Cell Nucleus, Electrophoretic Mobility Shift Assay, Nerve Tissue Proteins, Restriction Fragment Mapping, Research and Analysis Methods, Biochemistry, Cell Line, ADAM10 Protein, Amyloid beta-Protein Precursor, Protein Domains, Humans, Protein Interaction Domains and Motifs, Fractionation, Phosphorylation, Post-Translational Modification, Molecular Biology Techniques, Molecular Biology, Sequence Deletion, Neurons, Gene Mapping, Deletion Mutagenesis, Phosphatases, Membrane Proteins, Nuclear Proteins, Biology and Life Sciences, Proteins, Cell Biology, Enzymes, Separation Processes, Mutagenesis, Proteolysis, Enzymology, Amyloid Precursor Protein Secretases, Cellular Structures and Organelles, Protein Processing, Post-Translational, Research Article
Abstract

Fe65 is an adaptor protein involved in both processing and signaling of the Alzheimer-associated amyloid-β 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 γ-secretase inhibitors decreased nuclear Fe65 in a similar way indicating an important role also of α-secretase in regulating nuclear translocation.

Published
2016

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