Modulation of BAG3 expression and proteasomal activity by sAPPα does not require membrane-tethered holo-APP

Maintenance of intracellular proteostasis is essential for neuronal function, and emerging data support the view that disturbed proteostasis plays an important role in brain aging and the pathogenesis of age-related neurodegenerative disorders such as Alzheimer’s disease (AD). sAPPalpha (sAPPα), the...

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Main Authors: Kundu, Arpita (Author) , Milosch, Nelli (Author) , Antonietti, Patrick (Author) , Baumkötter, Frederik (Author) , Zymny, Andreas (Author) , Müller, Ulrike C. (Author) , Kins, Stefan (Author) , Hajieva, Parvana (Author) , Behl, Christian (Author) , Kögel, Donat (Author)
Format: Article (Journal)
Language:English
Published: 2016
In: Molecular neurobiology
Year: 2015, Volume: 53, Issue: 9, Pages: 5985-5994
ISSN:1559-1182
DOI:10.1007/s12035-015-9501-y
Online Access:Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1007/s12035-015-9501-y
Verlag, lizenzpflichtig, Volltext: https://link.springer.com/article/10.1007%2Fs12035-015-9501-y
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Author Notes:Arpita Kundu, Nelli Milosch, Patrick Antonietti, Frederik Baumkötter, Andreas Zymny, Ulrike C. Müller, Stefan Kins, Parvana Hajieva, Christian Behl, Donat Kögel
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Summary:Maintenance of intracellular proteostasis is essential for neuronal function, and emerging data support the view that disturbed proteostasis plays an important role in brain aging and the pathogenesis of age-related neurodegenerative disorders such as Alzheimer’s disease (AD). sAPPalpha (sAPPα), the extracellularly secreted N-terminal alpha secretase cleavage product of the amyloid precursor protein (APP), has an established function in neuroprotection. Recently, we provided evidence that membrane-bound holo-APP functionally cooperates with sAPPα to mediate neuroprotection via activation of the Akt survival signaling pathway and sAPPα directly affects proteostasis. Here, we demonstrate that in addition to its anti-apoptotic function, sAPPα has effects on neuronal proteostasis under conditions of proteasomal stress.
Item Description:Published online: 2 November 2015
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Physical Description:Online Resource
ISSN:1559-1182
DOI:10.1007/s12035-015-9501-y