Membrane tethering of APP c-terminal fragments is a prerequisite for T668 phosphorylation preventing nuclear sphere generation

A central molecular hallmark of Alzheimer's disease (AD) is the β- and γ-secretase-mediated cleavage of the amyloid precursor protein (APP), which causes the generation of different c-terminal fragments like C99, AICD57, or AICD50 that fully or in part contain the APP transmembrane domain. In t...

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Veröffentlicht in:	Cellular signalling 2016-11, Vol.28 (11), p.1725-1734
Hauptverfasser:	Bukhari, Hassan, Kolbe, Katharina, Leonhardt, Gregor, Loosse, Christina, Schröder, Elisabeth, Knauer, Shirley, Marcus, Katrin, Müller, Thorsten
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer Disease - metabolism Alzheimer Disease - pathology Amyloid beta-Protein Precursor - chemistry Amyloid beta-Protein Precursor - metabolism Amyloid Precursor Protein Secretases - metabolism Cell Line Cell Membrane - metabolism Cell Nucleus - metabolism Humans Mitogen-Activated Protein Kinase 10 - metabolism Models, Biological Phosphorylation Phosphothreonine - metabolism Plaque, Amyloid - metabolism Plaque, Amyloid - pathology Protein Binding
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