The APP intracellular domain is required for normal synaptic morphology, synaptic plasticity, and hippocampus-dependent behavior
The amyloid precursor protein family (APP/APLPs) has essential roles for neuromuscular synapse development and for the formation and plasticity of synapses within the CNS. Despite this, it has remained unclear whether APP mediates its functions primarily as a cell surface adhesion and signaling mole...
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| Hauptverfasser: | , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
December 9, 2015
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| In: |
The journal of neuroscience
Year: 2015, Jahrgang: 35, Heft: 49, Pages: 16018-16033 |
| ISSN: | 1529-2401 |
| DOI: | 10.1523/JNEUROSCI.2009-15.2015 |
| Online-Zugang: | Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1523/JNEUROSCI.2009-15.2015 Verlag, lizenzpflichtig, Volltext: https://www.jneurosci.org/content/35/49/16018 
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| Verfasserangaben: | Maja Klevanski, Ulrike Herrmann, Sascha W. Weyer, Romain Fol, Nathalie Cartier, David P. Wolfer, John H. Caldwell, Martin Korte, and Ulrike C. Müller |
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| 520 | |a The amyloid precursor protein family (APP/APLPs) has essential roles for neuromuscular synapse development and for the formation and plasticity of synapses within the CNS. Despite this, it has remained unclear whether APP mediates its functions primarily as a cell surface adhesion and signaling molecule or via its numerous proteolytic cleavage products. To address these questions, we followed a genetic approach and used APPΔCT15 knockin mice lacking the last 15 amino acids of APP, including the highly conserved YENPTY protein interaction motif. | ||
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